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Relevant bibliographies by topics / Branched peptide

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Journal articles

Academic literature on the topic 'Branched peptide'

Author: Grafiati

Published: 14 March 2023

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Journal articles on the topic "Branched peptide"

1

Eggimann, Gabriela A., Emilyne Blattes, Stefanie Buschor, et al. "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 (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 pro

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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 (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 (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 immun

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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, et al. "Peptide Nanovesicles Formed by the Self-Assembly of Branched Amphiphilic Peptides." PLoS ONE 7, no. 9 (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 (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

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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 (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, 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 (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

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