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Journal articles on the topic 'Branched peptide'

Author: Grafiati

Published: 14 March 2023

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1

Eggimann, Gabriela A., Emilyne Blattes, Stefanie Buschor, Rasomoy Biswas, Stephan M. Kammer, Tamis Darbre, and Jean-Louis Reymond. "Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells." Chem. Commun. 50, no. 55 (2014): 7254–57. http://dx.doi.org/10.1039/c4cc02780a.

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Redesigning linear cell penetrating peptides (CPPs) into a multi-branched topology with short dipeptide branches gave cell penetrating peptide dendrimers (CPPDs) with higher cell penetration, lower toxicity and hemolysis and higher serum stability than linear CPPs.

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2

Gudlur, Sushanth, Xiao Yao, Yasuaki Hiromasa, Takeo Iwamoto, and John M. Tomich. "Peptide Nanovesicles: Supramolecular Assembly of Branched Amphipathic Peptides." Biophysical Journal 100, no. 3 (February 2011): 388a. http://dx.doi.org/10.1016/j.bpj.2010.12.2304.

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3

Yang, Dongsik, Hongjian He, and Bing Xu. "Enzyme-instructed morphological transition of the supramolecular assemblies of branched peptides." Beilstein Journal of Organic Chemistry 16 (November 4, 2020): 2709–18. http://dx.doi.org/10.3762/bjoc.16.221.

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Here, we report the use of an enzymatic reaction to cleave the branch off branched peptides for inducing the morphological transition of the assemblies of the peptides. The attachment of DEDDDLLI sequences to the ε-amine of the lysine residue of a tetrapeptide produces branched peptides that form micelles. Upon the proteolytic cleavage of the branch, catalyzed by proteinase K, the micelles turn into nanofibers. We also found that the acetylation of the N-terminal of the branch increased the stability of the branched peptides. Moreover, these branched peptides facilitate the delivery of the proteins into cells. This work contributes insights for the development of peptide supramolecular assemblies via enzymatic noncovalent synthesis in cellular environment.

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4

SPETZLER, JANE C., and JAMES P. TAM. "Unprotected peptides as building blocks for branched peptides and peptide dendrimers." International Journal of Peptide and Protein Research 45, no. 1 (January 12, 2009): 78–85. http://dx.doi.org/10.1111/j.1399-3011.1995.tb01570.x.

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5

Plaué, S., S. Muller, and M. H. van Regenmortel. "A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies." Journal of Experimental Medicine 169, no. 5 (May 1, 1989): 1607–17. http://dx.doi.org/10.1084/jem.169.5.1607.

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Two peptides of eight (T2) and 10 (T1) residues corresponding to the branched moiety of ubiquitinated histone H2A have been synthesized and used for raising specific antibodies in rabbits. Antisera to peptide T1 reacted in ELISA with T1 and with H2A but not with ubiquitin; antisera to peptide T2 reacted with T2 but not with H2A or ubiquitin. When tested in immunoblotting, both peptide antisera reacted with ubiquitinated H2A but not with unconjugated H2A or with ubiquitin. Sera from patients with systemic lupus erythematosus (SLE) were shown previously to react with ubiquitin in ELISA and immunoblotting. When tested for their ability to react in ELISA with synthetic peptides T1 and T2, 96% of the SLE sera (diluted 1:500) that recognized ubiquitin also reacted with peptide T2. Of the SLE sera that did not react with ubiquitin, only 13% possessed antibodies able to bind peptide T2. Antibodies from seven SLE sera, purified on a T2-immunoadsorbent column, were also able to react either with H2A, and in three cases also with ubiquitin.

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6

Wang, Jian-Xun, Yi-Xiao Zhang, Jiang-Lan Li, Xiao-Ding Xu, Ren-Xi Zhuo, and Xian-Zheng Zhang. "Branched peptide fibers self-assembled from gemini-like amphiphilic peptides." Soft Matter 8, no. 37 (2012): 9523. http://dx.doi.org/10.1039/c2sm26136g.

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7

Gudlur, Sushanth, Pinakin Sukthankar, Jian Gao, L. Adriana Avila, Yasuaki Hiromasa, Jianhan Chen, Takeo Iwamoto, and John M. Tomich. "Peptide Nanovesicles Formed by the Self-Assembly of Branched Amphiphilic Peptides." PLoS ONE 7, no. 9 (September 18, 2012): e45374. http://dx.doi.org/10.1371/journal.pone.0045374.

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8

Kersten, Roland D., and Jing-Ke Weng. "Gene-guided discovery and engineering of branched cyclic peptides in plants." Proceedings of the National Academy of Sciences 115, no. 46 (October 29, 2018): E10961—E10969. http://dx.doi.org/10.1073/pnas.1813993115.

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The plant kingdom contains vastly untapped natural product chemistry, which has been traditionally explored through the activity-guided approach. Here, we describe a gene-guided approach to discover and engineer a class of plant ribosomal peptides, the branched cyclic lyciumins. Initially isolated from the Chinese wolfberry Lycium barbarum, lyciumins are protease-inhibiting peptides featuring an N-terminal pyroglutamate and a macrocyclic bond between a tryptophan-indole nitrogen and a glycine α-carbon. We report the identification of a lyciumin precursor gene from L. barbarum, which encodes a BURP domain and repetitive lyciumin precursor peptide motifs. Genome mining enabled by this initial finding revealed rich lyciumin genotypes and chemotypes widespread in flowering plants. We establish a biosynthetic framework of lyciumins and demonstrate the feasibility of producing diverse natural and unnatural lyciumins in transgenic tobacco. With rapidly expanding plant genome resources, our approach will complement bioactivity-guided approaches to unlock and engineer hidden plant peptide chemistry for pharmaceutical and agrochemical applications.

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9

Le, Zhiping, Wei Huang, Xiaobo Tian, Pengqiu Yu, and Yubo Tang. "Aspartic Acid Side-Chain Benzyl Ester as a Multifunctionalization Precursor for Synthesis of Branched and Cyclic Arginylglycylaspartic Acid Peptides." Synlett 28, no. 15 (June 29, 2017): 1966–70. http://dx.doi.org/10.1055/s-0036-1588870.

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Here, we report a peptide aspartic acid side-chain benzyl ester as a useful precursor that can be efficiently converted into various functional groups, including acid, amide, carbonyl hydrazide, carbonyl azide, or thio ester groups, without other protection for the peptide. With this strategy, we synthesized a series of novel branched and cyclic arginylglycylaspartic acid peptides through successive peptide C-terminal ligation and side-chain ligation based on a side-chain carbonyl azide or thio ester.

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10

Pini, Alessandro, Ylenia Runci, Chiara Falciani, Barbara Lelli, Jlenia Brunetti, Silvia Pileri, Monica Fabbrini, et al. "Stable peptide inhibitors prevent binding of lethal and oedema factors to protective antigen and neutralize anthrax toxin in vivo." Biochemical Journal 395, no. 1 (March 15, 2006): 157–63. http://dx.doi.org/10.1042/bj20051747.

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The lethal and oedema toxins produced by Bacillus anthracis, the aetiological agent of anthrax, are made by association of protective antigen with lethal and oedema factors and play a major role in the pathogenesis of anthrax. In the present paper, we describe the production of peptide-based specific inhibitors in branched form which inhibit the interaction of protective antigen with lethal and oedema factors and neutralize anthrax toxins in vitro and in vivo. Anti-protective antigen peptides were selected from a phage library by competitive panning with lethal factor. Selected 12-mer peptides were synthesized in tetra-branched form and were systematically modified to obtain peptides with higher affinity and inhibitory efficiency.

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11

McDonald, Tom O., Honglei Qu, Brian R. Saunders, and Rein V. Ulijn. "Branched peptide actuators for enzyme responsive hydrogel particles." Soft Matter 5, no. 8 (2009): 1728. http://dx.doi.org/10.1039/b818174h.

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12

Xiao, Anshan, Jie Yang, Yuping Feng, Shengli Cao, and Yufen Zhao. "Hydrolysis of DNA by N-Phosphoryl Branched Peptide." Phosphorus, Sulfur, and Silicon and the Related Elements 180, no. 8 (August 1, 2005): 1947–51. http://dx.doi.org/10.1080/104265090902705.

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13

Hebert, Elvira María, Gianfranco Mamone, Gianluca Picariello, Raúl R. Raya, Graciela Savoy, Pasquale Ferranti, and Francesco Addeo. "Characterization of the Pattern of αs1- and β-Casein Breakdown and Release of a Bioactive Peptide by a Cell Envelope Proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581." Applied and Environmental Microbiology 74, no. 12 (April 18, 2008): 3682–89. http://dx.doi.org/10.1128/aem.00247-08.

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ABSTRACT The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEPI/III variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the αs1- and β-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of αs1- and β-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized.

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14

Lorenzón, E. N., G. F. Cespedes, E. F. Vicente, L. G. Nogueira, T. M. Bauab, M. S. Castro, and E. M. Cilli. "Effects of Dimerization on the Structure and Biological Activity of Antimicrobial Peptide Ctx-Ha." Antimicrobial Agents and Chemotherapy 56, no. 6 (March 5, 2012): 3004–10. http://dx.doi.org/10.1128/aac.06262-11.

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ABSTRACTIt is well known that cationic antimicrobial peptides (cAMPs) are potential microbicidal agents for the increasing problem of antimicrobial resistance. However, the physicochemical properties of each peptide need to be optimized for clinical use. To evaluate the effects of dimerization on the structure and biological activity of the antimicrobial peptide Ctx-Ha, we have synthesized the monomeric and three dimeric (Lys-branched) forms of the Ctx-Ha peptide by solid-phase peptide synthesis using a combination of 9-fluorenylmethyloxycarbonyl (Fmoc) andt-butoxycarbonyl (Boc) chemical approaches. The antimicrobial activity assay showed that dimerization decreases the ability of the peptide to inhibit growth of bacteria or fungi; however, the dimeric analogs displayed a higher level of bactericidal activity. In addition, a dramatic increase (50 times) in hemolytic activity was achieved with these analogs. Permeabilization studies showed that the rate of carboxyfluorescein release was higher for the dimeric peptides than for the monomeric peptide, especially in vesicles that contained sphingomyelin. Despite different biological activities, the secondary structure and pore diameter were not significantly altered by dimerization. In contrast to the case for other dimeric cAMPs, we have shown that dimerization selectively decreases the antimicrobial activity of this peptide and increases the hemolytic activity. The results also show that the interaction between dimeric peptides and the cell wall could be responsible for the decrease of the antimicrobial activity of these peptides.

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15

Liu, Zhihui, Moyi Li, Dafu Cui, and Jian Fei. "Macro-branched cell-penetrating peptide design for gene delivery." Journal of Controlled Release 102, no. 3 (February 2005): 699–710. http://dx.doi.org/10.1016/j.jconrel.2004.10.013.

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16

Zhang, Jerry G., Oren Krajden, Rajesh K. Kainthan, Jayachandran N. Kizhakkedathu, and Maria I. C. Gyongyossy-Issa. "RGD-Substituted High Molecular Weight Hyper-Branched Polyglycerols (HPG) Are Effective Platelet Inhibitors." Blood 110, no. 11 (November 16, 2007): 925. http://dx.doi.org/10.1182/blood.v110.11.925.925.

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Abstract Peptides containing Arg-Gly-Asp (RGD) sequences are known to bind to integrins which mediate cell adhesion and therefore have been utilized in applications such as antithrombotics and tissue engineering. Although RGD and related peptides show promise, their unfavourable pharmacokinetic profiles and susceptibility to in vivo proteolysis hinder their clinical usefulness. Peptide-polymer conjugates can address one of these challenges by extending the peptide’s residence in plasma. Hyperbranched polyglycerols (HPGs) are biocompatible polyether polyols with very long plasma circulation half-lives (t1/2 ∼ 60h) and as such are ideally suited to be carriers in such conjugates. HPGs of three different molecular weights were conjugated with RGD peptides at various substitution levels. Some of the terminal hydroxyl groups of polyglycerols were converted to vinyl sulfone groups which were subsequently utilized to couple cysteine terminated RGD peptides. The following conjugates were made: 515 kDa with substitution levels of 100:1, 500:1 and 1000:1; 100 kDa with substitution levels of 100:1 and 1000:1; and 3 kDa with substitution levels of 1:1, and 10:1. RGD-coupled HPG inhibited fibrinogen binding to platelet glycoprotein IIb-IIIa as detected by flow cytometry using anti-fibrinogen. Compared to free RGD (Ic50 = 5 x 10-5 M), inhibition of fibrinogen binding increased with increasing HPG molecular weight and increasing RGD-substitution for the high MW conjugates: Ic50 for the 515 kDa conjugates were 6.3 x 10−8 M for the 100:1 substitution, 4.7 x 10-8 M for the 500:1 substitution, and 4.1 x 10−8 M for 1000:1 substitution; Ic50 for the 100 kDa conjugates were 7.0 x 10−7 M for the 100:1 substitution and 1.2 x 10−7 M for the 1000:1 substitution. Ic50 for the 3 kDa conjugates were 2 x 10−5 M for the 1:1 substitution, 2 x 10−4 M for 10:1 substitution. Similarly, platelet function, as demonstrated by MnCl2-initated aggregation was inhibited in a dose- and molecular weight-dependent manner by HPG-RGD conjugates. Platelet aggregate formation and aggregate size were confirmed by microscopy. However, unsubstituted HPG had no effect on platelet fibrinogen binding and neither conjugated nor unconjugated HPG increased platelet CD62 surface expression. Trypsin digestion (but not SBTI-treated trypsin) removed the inhibitory activity of the conjugates and thus confirmed that both fibrinogen binding and aggregation-inhibition were dependent on the RGD peptide sequence. Such multi-determinant peptide-HPG conjugates represent a new approach to the development of antithrombotic drugs.

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17

Brunetti, Jlenia, Chiara Falciani, Barbara Lelli, Andrea Minervini, Niccolò Ravenni, Lorenzo Depau, Giampaolo Siena, et al. "Neurotensin Branched Peptide as a Tumor-Targeting Agent for Human Bladder Cancer." BioMed Research International 2015 (2015): 1–7. http://dx.doi.org/10.1155/2015/173507.

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Despite recent advances in multimodal therapy, bladder cancer still ranks ninth in worldwide cancer incidence. New molecules which might improve early diagnosis and therapeutic efficiency for tumors of such high epidemiological impact therefore have very high priority. In the present study, the tetrabranched neurotensin peptide NT4 was conjugated with functional units for cancer-cell imaging or therapy and was tested on bladder cancer cell lines and specimens from bladder cancer surgical resections, in order to evaluate its potential for targeted personalized therapy of bladder cancer. Fluorophore-conjugated NT4 distinguished healthy and cancer tissues with good statistical significanceP<0.05. NT4 conjugated to methotrexate or gemcitabine was cytotoxic for human bladder cancer cell lines at micromolar concentrations. Their selectivity for bladder cancer tissue and capacity to carry tracers or drugs make NT4 peptides candidate tumor targeting agents for tracing cancer cells and for personalized therapy of human bladder cancer.

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18

Moslah, Wassim, Dorra Aissaoui-Zid, Soioulata Aboudou, Zaineb Abdelkafi-Koubaa, Marie Potier-Cartereau, Aude Lemettre, Ines ELBini-Dhouib, et al. "Strengthening Anti-Glioblastoma Effect by Multi-Branched Dendrimers Design of a Scorpion Venom Tetrapeptide." Molecules 27, no. 3 (January 26, 2022): 806. http://dx.doi.org/10.3390/molecules27030806.

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Glioblastoma is the most aggressive and invasive form of central nervous system tumors due to the complexity of the intracellular mechanisms and molecular alterations involved in its progression. Unfortunately, current therapies are unable to stop its neoplastic development. In this context, we previously identified and characterized AaTs-1, a tetrapeptide (IWKS) from Androctonus autralis scorpion venom, which displayed an anti-proliferative effect against U87 cells with an IC50 value of 0.57 mM. This peptide affects the MAPK pathway, enhancing the expression of p53 and altering the cytosolic calcium concentration balance, likely via FPRL-1 receptor modulation. In this work, we designed and synthesized new dendrimers multi-branched molecules based on the sequence of AaTs-1 and showed that the di-branched (AaTs-1-2B), tetra-branched (AaTs-1-4B) and octo-branched (AaTs-1-8B) dendrimers displayed 10- to 25-fold higher effects on the proliferation of U87 cells than AaTs-1. We also found that the effects of the newly designed molecules are mediated by the enhancement of the ERK1/2 and AKT phosphorylated forms and by the increase in p53 expression. Unlike AaTs-1, AaTs-1-8B and especially AaTs-1-4B affected the migration of the U87 cells. Thus, the multi-branched peptide synthesis strategy allowed us to make molecules more active than the linear peptide against the proliferation of U87 glioblastoma cells.

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19

Guo, Jiaqi, Hongjian He, Beom Jin Kim, Jiaqing Wang, Meihui Yi, Cheng Lin, and Bing Xu. "The ratio of hydrogelator to precursor controls the enzymatic hydrogelation of a branched peptide." Soft Matter 16, no. 44 (2020): 10101–5. http://dx.doi.org/10.1039/d0sm00867b.

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Here, we report an apparently counterintuitive observation, in which a lower volume fraction of a branched peptide forms a stronger hydrogel after an enterokinase (ENTK) cleaves off the branch from the peptide.

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20

Ceccherini, Federica, Chiara Falciani, Martina Onori, Silvia Scali, Simona Pollini, Gian Maria Rossolini, Luisa Bracci, and Alessandro Pini. "Antimicrobial activity of levofloxacin – M33 peptide conjugation or combination." MedChemComm 7, no. 2 (2016): 258–62. http://dx.doi.org/10.1039/c5md00392j.

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21

Du, Mingxuan, Yong Bu, Yan Zhou, Yurong Zhao, Shengjie Wang, and Hai Xu. "Peptide-templated synthesis of branched MnO2 nanowires with improved electrochemical performances." RSC Advances 7, no. 21 (2017): 12711–18. http://dx.doi.org/10.1039/c7ra00829e.

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22

Zhang, Luhao, Jianlei Shen, Ting Wang, Kun Wang, Nan Chen, Haiyun Song, Xiuhai Mao, et al. "Branched Nanostructure for Dual-Model Imaging." Nano LIFE 07, no. 02 (May 11, 2017): 1750003. http://dx.doi.org/10.1142/s1793984417500039.

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Single-model imaging can hardly provide sufficient information to clearly describe cellular behaviors, thus dual-model probes have been intensively studied for multiplex bio-detection and bio-imaging. Here, we developed a series of branched Au nanostructures with different surface modifications, which enabled dark-field microscopy (DFM) and surface-enhanced Raman scattering (SERS) imaging, owning to their high electromagnetic fields around the nanostructures. Moreover, we found that nanostructures modified with DNA and Arg–Gly–Asp (RGD) peptide could be internalized by cells efficiently and well distributed in cells without aggregation. These results demonstrate the potential of the nanostructures in applications like cell imaging and drug delivery.

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23

Johnson, Quentin R., Richard J. Lindsay, Sherin R. Raval, Jeremy S. Dobbs, Ricky B. Nellas, and Tongye Shen. "Effects of Branched O-Glycosylation on a Semiflexible Peptide Linker." Journal of Physical Chemistry B 118, no. 8 (February 18, 2014): 2050–57. http://dx.doi.org/10.1021/jp410788r.

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24

Frutos, Silvia, Michael Goger, Baldissera Giovani, David Cowburn, and Tom W. Muir. "Branched intermediate formation stimulates peptide bond cleavage in protein splicing." Nature Chemical Biology 6, no. 7 (May 23, 2010): 527–33. http://dx.doi.org/10.1038/nchembio.371.

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25

Kepple, K. V., N. Patel, P. Salamon, and A. M. Segall. "Interactions between branched DNAs and peptide inhibitors of DNA repair." Nucleic Acids Research 36, no. 16 (August 1, 2008): 5319–34. http://dx.doi.org/10.1093/nar/gkn512.

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26

Xiao, Anshan, Yuping Feng, Shengli Cao, Wenjun Xie, and Yufen Zhao. "Hydrolysis of DNA by a Branched Peptide without Aromatic Residues." International Journal of Peptide Research and Therapeutics 11, no. 3 (September 2005): 181–83. http://dx.doi.org/10.1007/s10989-005-6788-y.

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27

Tung, Ching-Hsuan, Luisa Quinti, Farouc A. Jaffer, and Ralph Weissleder. "A Branched Fluorescent Peptide Probe for Imaging of Activated Platelets." Molecular Pharmaceutics 2, no. 1 (December 21, 2004): 92–95. http://dx.doi.org/10.1021/mp0499048.

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28

Sukthankar, Pinakin, Susan K. Whitaker, Macy Garcia, Alvaro Herrera, Mark Boatwright, Om Prakash, and John M. Tomich. "Thermally Induced Conformational Transitions in Nascent Branched Amphiphilic Peptide Capsules." Langmuir 31, no. 10 (March 6, 2015): 2946–55. http://dx.doi.org/10.1021/la504381y.

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29

Koga, Tomoyuki, Harunobu Matsui, Takahiro Matsumoto, and Nobuyuki Higashi. "Shape-specific nanofibers via self-assembly of three-branched peptide." Journal of Colloid and Interface Science 358, no. 1 (June 2011): 81–85. http://dx.doi.org/10.1016/j.jcis.2011.02.055.

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30

Gunderson, Carl W., Jeffrey L. Boldt, R. Nathan Authement, and Anca M. Segall. "Peptide wrwycr Inhibits the Excision of Several Prophages and Traps Holliday Junctions inside Bacteria." Journal of Bacteriology 191, no. 7 (January 30, 2009): 2169–76. http://dx.doi.org/10.1128/jb.01559-08.

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ABSTRACT Peptide inhibitors of phage lambda site-specific recombination were previously isolated by screening synthetic combinatorial peptide libraries. These inhibitors cause the accumulation of complexes between the recombinase and the Holliday junction intermediate of several highly divergent tyrosine recombinases. Peptide WRWYCR and its d-amino acid derivative bind to the center of protein-free junctions and prevent their resolution either by site-specific recombinases or by junction resolvases or helicases. With lesser affinity, the peptides also bind to branched DNA molecules that mimic replication forks. The peptides are bactericidal to both gram-positive and gram-negative bacteria, presumably because they can interfere with DNA repair and with chromosome dimer resolution by the XerC and XerD tyrosine recombinases. In order to test the correspondence between their mechanism in vivo and in vitro, we have tested and shown peptide wrwycr's ability to inhibit the excision of several prophages (lambda, P22, Gifsy-1, Gifsy-2, Fels-1, Fels-2) and to trap Holliday junction intermediates of phage lambda site-specific recombination in vivo. In addition, we found that the peptide inhibits replication of the Salmonella prophage Fels-1 while integrated in the chromosome. These findings further support the proposed mechanistic basis for the antimicrobial activity of the peptide and its use as a tool to dissect strand exchange-dependent DNA repair within cells.

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31

Szyrwiel, Łukasz, Mari Shimura, Junko Shirataki, Satoshi Matsuyama, Akihiro Matsunaga, Bartosz Setner, Łukasz Szczukowski, et al. "A novel branched TAT47–57peptide for selective Ni2+introduction into the human fibrosarcoma cell nucleus." Metallomics 7, no. 7 (2015): 1155–62. http://dx.doi.org/10.1039/c5mt00021a.

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32

Brooks, Nicole, Jennifer Hsu, Sandra Esparon, Dodie Pouniotis, and Geoffrey Pietersz. "Immunogenicity of a Tripartite Cell Penetrating Peptide Containing a MUC1 Variable Number of Tandem Repeat (VNTR) and A T Helper Epitope." Molecules 23, no. 9 (September 2, 2018): 2233. http://dx.doi.org/10.3390/molecules23092233.

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Peptide-based vaccines for cancer have many advantages however, for optimization these immunogens should incorporate peptide epitopes that induce CD8, as well as CD4 responses, antibody and long term immunity. Cell penetrating peptides (CPP) with a capacity of cytosolic delivery have been used to deliver antigenic peptides and proteins to antigen presenting cells to induce cytotoxic T cell, helper T cell and humoral responses in mice. For this study, a tripartite CPP including a mucin 1 (MUC1) variable number of tandem repeat (VNTR) containing multiple T cell epitopes and tetanus toxoid universal T helper epitope peptide (tetCD4) was synthesised (AntpMAPMUC1tet) and immune responses investigated in mice. Mice vaccinated with AntpMAPMUC1tet + CpG show enhanced antigen-specific interferon-gamma (IFN-γ) and IL-4 T cell responses compared with AntpMAPMUC1tet vaccination alone and induced a Th1 response, characterised by a higher ratio of IgG2a antibody/IgG1 antibodies. Furthermore, vaccination generated long term MUC1-specific antibody and T cell responses and delayed growth of MUC1+ve tumours in mice. This data demonstrates the efficient delivery of branched multiple antigen peptides incorporating CPP and that the addition of CpG augments immune responses.

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33

Szyrwiel, Łukasz, Dávid Lukács, Dávid F. Srankó, Zsolt Kerner, Aleksandra Kotynia, Justyna Brasuń, Bartosz Setner, Zbigniew Szewczuk, Katarzyna Malec, and József S. Pap. "Armed by Asp? C-terminal carboxylate in a Dap-branched peptide and consequences in the binding of CuII and electrocatalytic water oxidation." RSC Advances 7, no. 40 (2017): 24657–66. http://dx.doi.org/10.1039/c7ra03814c.

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34

Perugini, Valeria, and Matteo Santin. "The Real-Time Validation of the Effectiveness of Third-Generation Hyperbranched Poly(ɛ-lysine) Dendrons-Modified KLVFF Sequences to Bind Amyloid-β1-42 Peptides Using an Optical Waveguide Light-Mode Spectroscopy System." Sensors 22, no. 23 (December 6, 2022): 9561. http://dx.doi.org/10.3390/s22239561.

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The aggregation of cytotoxic amyloid peptides (Aβ1-42) is widely recognised as the cause of brain tissue degeneration in Alzheimer’s disease (AD). Indeed, evidence indicates that the deposition of cytotoxic Aβ1-42 plaques formed through the gradual aggregation of Aβ1-42 monomers into fibrils determines the onset of AD. Thus, distinct Aβ1-42 inhibitors have been developed, and only recently, the use of short linear peptides has shown promising results by either preventing or reversing the process of Aβ1-42 aggregation. Among them, the KLVFF peptide sequence, which interacts with the hydrophobic region of Aβ16-20, has received widespread attention due to its ability to inhibit fibril formation of full-length Aβ1-42. In this study, hyperbranched poly-L-lysine dendrons presenting sixteen KLVFF at their uppermost molecular branches were designed with the aim of providing the KLVFF sequence with a molecular scaffold able to increase its stability and of improving Aβ1-42 fibril formation inhibitory effect. These high-purity branched KLVFF were used to functionalise the surface of the metal oxide chip of the optical waveguide lightmode spectroscopy sensor showing the more specific, accurate and rapid measurement of Aβ1-42 than that detected by linear KLVFF peptides.

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35

Wynn, Jessica E., Wenyu Zhang, Denis M. Tebit, Laurie R. Gray, Marie-Louise Hammarskjold, David Rekosh, and Webster L. Santos. "Effect of intercalator and Lewis acid–base branched peptide complex formation: boosting affinity towards HIV-1 RRE RNA." MedChemComm 7, no. 7 (2016): 1436–40. http://dx.doi.org/10.1039/c6md00171h.

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Lee, Duhwan, Yeong Mi Lee, Jihoon Kim, Myung Kyu Lee, and Won Jong Kim. "Enhanced tumor-targeted gene delivery by bioreducible polyethylenimine tethering EGFR divalent ligands." Biomaterials Science 3, no. 7 (2015): 1096–104. http://dx.doi.org/10.1039/c5bm00004a.

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Fatullaev, E. I., V. V. Bezrodnyi, and I. M. Neelov. "MD Simulation of AEDG Peptide Complexes with New K2R Dendrimer and Dendrigraft." International Journal of Biology and Biomedical Engineering 16 (January 3, 2022): 73–81. http://dx.doi.org/10.46300/91011.2022.16.9.

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Biocompatible peptide dendrimers and dendrigrafts have useful properties for application in biomedicine. In previous papers the computational approach for study lysine dendrimers and dendrigrafts as well as their complexes with various medical peptides was used. In this paper the comparison of complex formation between molecules of therapeutic AEDG tetrapeptide and novel K2R peptide dendrimer or DG2 dendrigraft of near the same size and charge was fulfilled. The systems consisting of 16 therapeutic AEDG tetrapeptide molecules and one dendrimer or one dendrigraft were studied by molecular dynamics simulation. Full atomic models of these molecules in water with explicit counterions were used for this goal. First of all, the process of complex formation was studied. It was obtained that peptide molecules were attracted by both branched molecules and were quickly adsorbed by them. Times of complexes formation as well as size, anisotropy and structure of each complex were calculated. It was demonstrated that both K2R dendrimer and DG2 dendrigraft are effective for complexation of these peptide molecules but new dendrimer complex is more stable than dendrigraft complex because it has almost twice more hydrogen bonds with peptide molecules and 33% more ion pairs with their charged groups.

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Liu, Chuan-Fa, and James P. Tam. "Synthesis of a symmetric branched peptide. Assembly of a cyclic peptide on a small tetraacetate template." Chemical Communications, no. 17 (1997): 1619–20. http://dx.doi.org/10.1039/a702129a.

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Welser, Katharina, Frederick Campbell, Laila Kudsiova, Atefeh Mohammadi, Natalie Dawson, Stephen L. Hart, David J. Barlow, Helen C. Hailes, M. Jayne Lawrence, and Alethea B. Tabor. "Gene Delivery Using Ternary Lipopolyplexes Incorporating Branched Cationic Peptides: The Role of Peptide Sequence and Branching." Molecular Pharmaceutics 10, no. 1 (December 4, 2012): 127–41. http://dx.doi.org/10.1021/mp300187t.

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Benjouad, A., E. Fenouillet, J. C. Gluckman, and J. M. Sabatier. "Multi-Branched Peptide Constructs (MBPC) of the V3 Loop of Envelope Glycoprotein gp120 Inhibit Human Immunodeficiency Virus-Induced Syncytium Formation." Antiviral Chemistry and Chemotherapy 5, no. 3 (June 1994): 195–96. http://dx.doi.org/10.1177/095632029400500310.

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The principle neutralizing domain of human immunodeficiency virus type-1 (HIV-1) envelope glycoprotein, the V3 region, is likely to be involved in HIV-mediated membrane fusion. While V3-derived monomeric peptides enhance HIV-1 infection through a CD4-dependent mechanism (DeRossi et al., 1991), the authors observed that multi-branched peptide constructs (MBPC) based on the V3 consensus sequence of European/North American isolates inhibited both HIV-1 and HIV-2 mediated syncytia at concentrations that did not alter cell viability nor blood lymphocyte allogeneic, antigen- or mitogen-induced proliferations. V3 MBPC bound to CD4+ cells and their binding was inhibited by soluble CD4 and by a benzylated peptide derived from its CDR3 region. These data indicate that V3-based MBPC may be used for delineating HIV entry mechanisms and might behave as antiviral agents of broad specificity.

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Bryson, David I., Wenyu Zhang, W. Keith Ray, and Webster L. Santos. "Screening of a branched peptide library with HIV-1 TAR RNA." Molecular BioSystems 5, no. 9 (2009): 1070. http://dx.doi.org/10.1039/b904304g.

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Koh, Ming Liang, Katrina A. Jolliffe, and Sébastien Perrier. "Hierarchical Assembly of Branched Supramolecular Polymers from (Cyclic Peptide)–Polymer Conjugates." Biomacromolecules 15, no. 11 (October 14, 2014): 4002–11. http://dx.doi.org/10.1021/bm501062d.

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Kaloyanova, S., M. Lelle, K. Müllen, and K. Peneva. "852: Branched cell-penetrating peptide drug conjugates for overcoming drug resistance." European Journal of Cancer 50 (July 2014): S207—S208. http://dx.doi.org/10.1016/s0959-8049(14)50755-1.

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Sukthankar, Pinakin, L. Adriana Avila, Susan K. Whitaker, Takeo Iwamoto, Alfred Morgenstern, Christos Apostolidis, Ke Liu, Robert P. Hanzlik, Ekaterina Dadachova, and John M. Tomich. "Branched amphiphilic peptide capsules: Cellular uptake and retention of encapsulated solutes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, no. 9 (September 2014): 2296–305. http://dx.doi.org/10.1016/j.bbamem.2014.02.005.

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Stavrakoudis, Athanassios, Sevasti Makropoulou, Vassilios Tsikaris, Maria Sakarellos-Daitsiotis, Constantinos Sakarellos, and Ioannis N. Demetropoulos. "Computational screening of branched cyclic peptide motifs as potential enzyme mimetics." Journal of Peptide Science 9, no. 3 (2003): 145–55. http://dx.doi.org/10.1002/psc.441.

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Harrington, Daniel A., Earl Y. Cheng, Mustafa O. Guler, Leslie K. Lee, Jena L. Donovan, Randal C. Claussen, and Samuel I. Stupp. "Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds." Journal of Biomedical Materials Research Part A 78A, no. 1 (July 2006): 157–67. http://dx.doi.org/10.1002/jbm.a.30718.

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Puszko, Anna K., Piotr Sosnowski, Dagmara Tymecka, Françoise Raynaud, Olivier Hermine, Yves Lepelletier, and Aleksandra Misicka. "Neuropilin-1 peptide-like ligands with proline mimetics, tested using the improved chemiluminescence affinity detection method." MedChemComm 10, no. 2 (2019): 332–40. http://dx.doi.org/10.1039/c8md00537k.

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Szyrwiel, Łukasz, József S. Pap, Łukasz Szczukowski, Zsolt Kerner, Justyna Brasuń, Bartosz Setner, Zbigniew Szewczuk, and Wiesław Malinka. "Branched peptide with three histidines for the promotion of CuII binding in a wide pH range – complementary potentiometric, spectroscopic and electrochemical studies." RSC Advances 5, no. 70 (2015): 56922–31. http://dx.doi.org/10.1039/c5ra08602g.

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Jones, S. M. A., and S. J. Yeaman. "Phosphorylation of branched-chain 2-oxo acid dehydrogenase complex in isolated adipocytes. Effects of 2-oxo acids." Biochemical Journal 236, no. 1 (May 15, 1986): 209–13. http://dx.doi.org/10.1042/bj2360209.

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Isolated adipocytes from rat epididymal fat-pads were incubated with [32P]Pi, and intracellular phosphoproteins were then analysed by SDS/polyacrylamide-gel electrophoresis and autoradiography. A phosphorylated polypeptide of apparent Mr 46,000 was identified as the alpha-subunit of branched-chain 2-oxo acid dehydrogenase complex by immunoprecipitation using antiserum raised against the homogeneous E1 component of branched-chain 2-oxo acid dehydrogenase complex. Immunoprecipitation of this phosphoprotein is blocked in a competitive manner by purified branched-chain 2-oxo acid dehydrogenase complex. Peptide mapping of the isolated phosphoprotein indicates that two sites on the polypeptide are phosphorylated in the intact cells. Addition of branched-chain 2-oxo acids to the incubation medium causes diminution in the extent of labelling of both phosphorylation sites on the alpha-subunit, an effect presumably mediated via their known inhibitory action on branched-chain 2-oxo acid dehydrogenase kinase. These observations provide direct evidence for phosphorylation of branched-chain 2-oxo acid dehydrogenase complex in intact cells.

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Díaz-Perlas, Cristina, Benjamí Oller-Salvia, Macarena Sánchez-Navarro, Meritxell Teixidó, and Ernest Giralt. "Branched BBB-shuttle peptides: chemoselective modification of proteins to enhance blood–brain barrier transport." Chemical Science 9, no. 44 (2018): 8409–15. http://dx.doi.org/10.1039/c8sc02415d.

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