Статті в журналах з теми "HETEROCHIRAL PEPTIDE"
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Mortenson, David E., Jay D. Steinkruger, Dale F. Kreitler, Dominic V. Perroni, Gregory P. Sorenson, Lijun Huang, Ritesh Mittal, et al. "High-resolution structures of a heterochiral coiled coil." Proceedings of the National Academy of Sciences 112, no. 43 (October 12, 2015): 13144–49. http://dx.doi.org/10.1073/pnas.1507918112.
Повний текст джерелаDemizu, Yosuke, Hiroko Yamashita, Takashi Misawa, Mitsunobu Doi, Makoto Oba, Masakazu Tanaka, and Masaaki Kurihara. "Handedness Preferences of Heterochiral Helical Peptides Containing Homochiral Peptide Segments." European Journal of Organic Chemistry 2016, no. 4 (January 5, 2016): 840–46. http://dx.doi.org/10.1002/ejoc.201501146.
Повний текст джерелаGoyal, Ruchika, Gaurav Jerath, Aneesh Chandrasekharan, T. R. Santhosh Kumar, and Vibin Ramakrishnan. "Peptide-based delivery vectors with pre-defined geometrical locks." RSC Medicinal Chemistry 11, no. 11 (2020): 1303–13. http://dx.doi.org/10.1039/d0md00229a.
Повний текст джерелаKovačević, Monika, Mojca Čakić Semenčić, Kristina Radošević, Krešimir Molčanov, Sunčica Roca, Lucija Šimunović, Ivan Kodrin, and Lidija Barišić. "Conformational Preferences and Antiproliferative Activity of Peptidomimetics Containing Methyl 1′-Aminoferrocene-1-carboxylate and Turn-Forming Homo- and Heterochiral Pro-Ala Motifs." International Journal of Molecular Sciences 22, no. 24 (December 16, 2021): 13532. http://dx.doi.org/10.3390/ijms222413532.
Повний текст джерелаMatsuda, Kenichi, Rui Zhai, Takahiro Mori, Masakazu Kobayashi, Ayae Sano, Ikuro Abe, and Toshiyuki Wakimoto. "Heterochiral coupling in non-ribosomal peptide macrolactamization." Nature Catalysis 3, no. 6 (May 4, 2020): 507–15. http://dx.doi.org/10.1038/s41929-020-0456-7.
Повний текст джерелаPark, Hae Sook, та Young Kee Kang. "Impact of aza-substitutions on the preference of helix handedness for β-peptide oligomers: a DFT study". RSC Advances 13, № 5 (2023): 3079–82. http://dx.doi.org/10.1039/d2ra07575j.
Повний текст джерелаAlkorta, Ibon, and José Elguero. "Theoretical study of peptide model dimers. Homo versus heterochiral complexes." Journal of Molecular Structure: THEOCHEM 680, no. 1-3 (July 2004): 191–98. http://dx.doi.org/10.1016/j.theochem.2004.04.030.
Повний текст джерелаXie, Yan-Yan, Xue-Qi Wang, Mei-Yan Sun, Xiao-Tong Qin, Xiao-Feng Su, Xiao-Fang Ma, Xiao-Zhi Liu, Cheng Zhong, and Shi-Ru Jia. "Heterochiral peptide-based biocompatible and injectable supramolecular hydrogel with antibacterial activity." Journal of Materials Science 57, no. 8 (February 2022): 5198–209. http://dx.doi.org/10.1007/s10853-022-06982-7.
Повний текст джерелаBirch, David, Michael North, Roger R. Hill, and G. E. Jeffs. "Stereochemical preference for heterochiral coupling controls selectivity in competitive peptide synthesis." Chemical Communications, no. 10 (1999): 941–42. http://dx.doi.org/10.1039/a901730e.
Повний текст джерелаRivera Islas, Jesús, Véronique Pimienta, Jean-Claude Micheau, and Thomas Buhse. "Kinetic analysis of artificial peptide self-replication. Part II: The heterochiral case." Biophysical Chemistry 103, no. 3 (March 2003): 201–11. http://dx.doi.org/10.1016/s0301-4622(02)00249-1.
Повний текст джерелаZerze, Gül H., Frank H. Stillinger та Pablo G. Debenedetti. "Effect of heterochiral inversions on the structure of a β‐hairpin peptide". Proteins: Structure, Function, and Bioinformatics 87, № 7 (18 березня 2019): 569–78. http://dx.doi.org/10.1002/prot.25680.
Повний текст джерелаCarlomagno, Tiziano, Maria C. Cringoli, Slavko Kralj, Marina Kurbasic, Paolo Fornasiero, Paolo Pengo, and Silvia Marchesan. "Biocatalysis of d,l-Peptide Nanofibrillar Hydrogel." Molecules 25, no. 13 (June 30, 2020): 2995. http://dx.doi.org/10.3390/molecules25132995.
Повний текст джерелаBirch, David, Roger R. Hill, G. E. Jeffs, and Michael North. "ChemInform Abstract: Stereochemical Preference for Heterochiral Coupling Controls Selectivity in Competitive Peptide Synthesis." ChemInform 30, no. 37 (June 13, 2010): no. http://dx.doi.org/10.1002/chin.199937212.
Повний текст джерелаMarchesan, S., K. E. Styan, C. D. Easton, L. Waddington, and A. V. Vargiu. "Higher and lower supramolecular orders for the design of self-assembled heterochiral tripeptide hydrogel biomaterials." Journal of Materials Chemistry B 3, no. 41 (2015): 8123–32. http://dx.doi.org/10.1039/c5tb00858a.
Повний текст джерелаKim, J. Dongun, Douglas H. Pike, Alexei M. Tyryshkin, G. V. T. Swapna, Hagai Raanan, Gaetano T. Montelione, Vikas Nanda, and Paul G. Falkowski. "Minimal Heterochiral de Novo Designed 4Fe–4S Binding Peptide Capable of Robust Electron Transfer." Journal of the American Chemical Society 140, no. 36 (August 24, 2018): 11210–13. http://dx.doi.org/10.1021/jacs.8b07553.
Повний текст джерелаSaha, Indranil, Bhaswati Chatterjee, Narayanaswamy Shamala, and Padmanabhan Balaram. "Crystal structures of peptide enantiomers and racemates: Probing conformational diversity in heterochiral Pro-Pro sequences." Biopolymers 90, no. 4 (2008): 537–43. http://dx.doi.org/10.1002/bip.20982.
Повний текст джерелаSpäth, Julia, Fiona Stuart, Luyong Jiang та John A Robinson. "Stabilization of aβ-Hairpin Conformation in a Cyclic Peptide Using the Templating Effect of a Heterochiral Diproline Unit". Helvetica Chimica Acta 81, № 9 (9 вересня 1998): 1726–38. http://dx.doi.org/10.1002/(sici)1522-2675(19980909)81:9<1726::aid-hlca1726>3.0.co;2-h.
Повний текст джерелаMakarević, Janja, Milan Jokić, Leo Frkanec, Vesna Čaplar, Nataša Šijaković Vujičić, and Mladen Žinić. "Oxalyl retro-peptide gelators. Synthesis, gelation properties and stereochemical effects." Beilstein Journal of Organic Chemistry 6 (October 4, 2010): 945–59. http://dx.doi.org/10.3762/bjoc.6.106.
Повний текст джерелаBhadbhade, Mohan M., and Raghuvansh Kishore. "Intramolecular CH···O Hydrogen-bond mediated stabilization of a Cis-DPro imide-bond in a stereocontrolled heterochiral model peptide." Biopolymers 97, no. 1 (August 19, 2011): 73–82. http://dx.doi.org/10.1002/bip.21705.
Повний текст джерелаNAGARAJAN, V., VASANTHA PATTABHI, A. JOHNSON, V. BOBDE, and S. DURANI. "Crystal structures of heterochiral peptides." Journal of Peptide Research 49, no. 1 (January 12, 2009): 74–79. http://dx.doi.org/10.1111/j.1399-3011.1997.tb01123.x.
Повний текст джерелаEGGLESTON, DRAKE S. "Heterochiral N-formyl methionyl peptides." International Journal of Peptide and Protein Research 31, no. 2 (January 12, 2009): 164–72. http://dx.doi.org/10.1111/j.1399-3011.1988.tb00019.x.
Повний текст джерелаMarchesan, S., C. D. Easton, K. E. Styan, L. J. Waddington, F. Kushkaki, L. Goodall, K. M. McLean, J. S. Forsythe, and P. G. Hartley. "Chirality effects at each amino acid position on tripeptide self-assembly into hydrogel biomaterials." Nanoscale 6, no. 10 (2014): 5172–80. http://dx.doi.org/10.1039/c3nr06752a.
Повний текст джерелаGuardiola, Salvador, Monica Varese, Xavier Roig, Macarena Sánchez-Navarro, Jesús García, and Ernest Giralt. "Target-templated de novo design of macrocyclic d-/l-peptides: discovery of drug-like inhibitors of PD-1." Chemical Science 12, no. 14 (2021): 5164–70. http://dx.doi.org/10.1039/d1sc01031j.
Повний текст джерелаFlorio, Daniele, Concetta Di Natale, Pasqualina Liana Scognamiglio, Marilisa Leone, Sara La Manna, Sarah Di Somma, Paolo Antonio Netti, Anna Maria Malfitano, and Daniela Marasco. "Self-assembly of bio-inspired heterochiral peptides." Bioorganic Chemistry 114 (September 2021): 105047. http://dx.doi.org/10.1016/j.bioorg.2021.105047.
Повний текст джерелаClover, Tara M., Conor L. O’Neill, Rajagopal Appavu, Giriraj Lokhande, Akhilesh K. Gaharwar, Ammon E. Posey, Mark A. White, and Jai S. Rudra. "Self-Assembly of Block Heterochiral Peptides into Helical Tapes." Journal of the American Chemical Society 142, no. 47 (April 27, 2020): 19809–13. http://dx.doi.org/10.1021/jacs.9b09755.
Повний текст джерелаNanda, Vikas, and William F. DeGrado. "Computational Design of Heterochiral Peptides against a Helical Target." Journal of the American Chemical Society 128, no. 3 (January 2006): 809–16. http://dx.doi.org/10.1021/ja054452t.
Повний текст джерелаMunegumi, Toratane, and Akira Shimoyama. "Separation of homochiral peptides and heterochiral peptides in the developement of homochirality." Origins of Life and Evolution of the Biosphere 26, no. 3-5 (October 1996): 388–89. http://dx.doi.org/10.1007/bf02459827.
Повний текст джерелаChatterjee, Bhaswati, Indranil Saha, Srinivasarao Raghothama, Subrayashastry Aravinda, Rajkishor Rai, Narayanaswamy Shamala, and Padmanabhan Balaram. "Designed Peptides with Homochiral and Heterochiral Diproline Templates as Conformational Constraints." Chemistry - A European Journal 14, no. 20 (July 7, 2008): 6192–204. http://dx.doi.org/10.1002/chem.200702029.
Повний текст джерелаLiu, Xinyu, та Samuel H. Gellman. "Comparisons of β‐Hairpin Propensity Among Peptides with Homochiral or Heterochiral Strands". ChemBioChem 22, № 18 (30 липня 2021): 2772–76. http://dx.doi.org/10.1002/cbic.202100324.
Повний текст джерелаJeena, M. T., Keunsoo Jeong, Eun Min Go, Yuri Cho, Seokyung Lee, Seongeon Jin, Suk-Won Hwang, et al. "Heterochiral Assembly of Amphiphilic Peptides Inside the Mitochondria for Supramolecular Cancer Therapeutics." ACS Nano 13, no. 10 (September 11, 2019): 11022–33. http://dx.doi.org/10.1021/acsnano.9b02522.
Повний текст джерелаBalamurugan, Dhayalan, та Kannoth M. Muraleedharan. "Conformational Switching in Heterochiral α,β2,3-Hybrid Peptides in Response to Solvent Polarity". European Journal of Organic Chemistry 2015, № 24 (20 липня 2015): 5321–25. http://dx.doi.org/10.1002/ejoc.201500534.
Повний текст джерелаKantharaju, Srinivasarao Raghothama, Upadhyayula Surya Raghavender, Subrayashastry Aravinda, Narayanaswamy Shamala, and Padmanabhan Balaram. "Conformations of heterochiral and homochiral proline-pseudoproline segments in peptides: Context dependentcis-transpeptide bond isomerization." Biopolymers 92, no. 5 (2009): 405–16. http://dx.doi.org/10.1002/bip.21207.
Повний текст джерелаMunegumi, Toratane, and Akira Shimoyama. "Development of homochiral peptides in the chemical evolutionary process: Separation of homochiral and heterochiral oligopeptides." Chirality 15, S1 (2003): S108—S115. http://dx.doi.org/10.1002/chir.10256.
Повний текст джерелаČakić Semenčić, Mojca, Ivan Kodrin, Lidija Barišić, Marko Nuskol, and Anton Meden. "Synthesis and Conformational Study of Monosubstituted Aminoferrocene-Based Peptides Bearing Homo- and Heterochiral Pro-Ala Sequences." European Journal of Inorganic Chemistry 2017, no. 2 (August 16, 2016): 306–17. http://dx.doi.org/10.1002/ejic.201600648.
Повний текст джерелаFabiola, G. Felcy, Vivek Bobde, L. Damodharan, Vasantha Pattabhi та S. Durani. "Conformational Preferences of Heterochiral Peptides. Crystal Structures of Heterochiral Peptides Boc-(D) Val-(D) Ala-Leu-Ala-OMe and Boc-Val-Ala-Leu-(D) Ala-OMe-Enhanced Stability of β-sheet Through C-H…O Hydrogen Bonds". Journal of Biomolecular Structure and Dynamics 18, № 4 (1 лютого 2001): 579–94. http://dx.doi.org/10.1080/07391102.2001.10506690.
Повний текст джерелаFavre, Michel, Kerstin Moehle, Luyong Jiang, Bernhard Pfeiffer, and John A. Robinson. "Structural Mimicry of Canonical Conformations in Antibody Hypervariable Loops Using Cyclic Peptides Containing a Heterochiral Diproline Template." Journal of the American Chemical Society 121, no. 12 (March 1999): 2679–85. http://dx.doi.org/10.1021/ja984016p.
Повний текст джерелаLee, Hye-soo, and Yong-beom Lim. "Slow-Motion Self-Assembly: Access to Intermediates with Heterochiral Peptides to Gain Control over Alignment Media Development." ACS Nano 14, no. 3 (February 14, 2020): 3344–52. http://dx.doi.org/10.1021/acsnano.9b09070.
Повний текст джерелаDemizu, Yosuke, Hiroko Yamashita, Mitsunobu Doi, Takashi Misawa, Makoto Oba, Masakazu Tanaka, and Masaaki Kurihara. "Topological Study of the Structures of Heterochiral Peptides Containing Equal Amounts of l-Leu and d-Leu." Journal of Organic Chemistry 80, no. 17 (August 22, 2015): 8597–603. http://dx.doi.org/10.1021/acs.joc.5b01541.
Повний текст джерелаKamada, Rui, Natsumi Nakagawa, Taiji Oyama, and Kazuyasu Sakaguchi. "Heterochiral Jun and Fos bZIP peptides form a coiled-coil heterodimer that is competent for DNA binding." Journal of Peptide Science 23, no. 7-8 (February 10, 2017): 644–49. http://dx.doi.org/10.1002/psc.2985.
Повний текст джерелаUdagawa, Hinako, Takato H. Yoneda, Ryo Masuda, and Takaki Koide. "A Strategy for Discovering Heterochiral Bioactive Peptides by Using the OB2 n P Library and SPOTs Method." ChemBioChem 20, no. 16 (July 15, 2019): 2070–73. http://dx.doi.org/10.1002/cbic.201900237.
Повний текст джерелаZhou, Yu, Chris Oostenbrink, Wilfred F. Van Gunsteren, Wilfred R. Hagen, Simon W. De Leeuw, and Jaap A. Jongejan *. "Relative stability of homochiral and heterochiral dialanine peptides. Effects of perturbation pathways and force-field parameters on free energy calculations." Molecular Physics 103, no. 14 (July 20, 2005): 1961–69. http://dx.doi.org/10.1080/00268970500096889.
Повний текст джерелаDi Blasio, Benedetto, Michele Saviano, Valerio Del Duca, Giuseppina De Simone, Filomena Rossi, Carlo Pedone, Ettore Benedetti, and Gian Paolo Lorenzi. "Conformational studies of heterochiral peptides with diastereoisomeric residues: Crystal and molecular structures of linear dipeptides derived from leucine, isoleucine, and allo-isoleucine." Biopolymers 36, no. 4 (October 1995): 401–8. http://dx.doi.org/10.1002/bip.360360403.
Повний текст джерелаRao, I. Nageshwara, Anima Boruah, S. Kiran Kumar, A. C. Kunwar, A. Sivalakshmi Devi, K. Vyas, Krishnan Ravikumar, and Javed Iqbal. "Synthesis and Conformational Studies of Novel Cyclic Peptides Constrained into a 310Helical Structure by a Heterochirald-Pro-l-Pro Dipeptide Template." Journal of Organic Chemistry 69, no. 6 (March 2004): 2181–84. http://dx.doi.org/10.1021/jo030282w.
Повний текст джерелаZhou, Yu, Chris Oostenbrink, Aldo Jongejan, Wilfred F. Van Gunsteren, Wilfred R. Hagen, Simon W. De Leeuw, and Jaap A. Jongejan. "Computational study of ground-state chiral induction in small peptides: Comparison of the relative stability of selected amino acid dimers and oligomers in homochiral and heterochiral combinations." Journal of Computational Chemistry 27, no. 7 (2006): 857–67. http://dx.doi.org/10.1002/jcc.20378.
Повний текст джерелаShao, Ning, Ling Yuan, Pengcheng Ma, Min Zhou, Ximian Xiao, Zihao Cong, Yueming Wu, Guohui Xiao, Jian Fei та Runhui Liu. "Heterochiral β-Peptide Polymers Combating Multidrug-Resistant Cancers Effectively without Inducing Drug Resistance". Journal of the American Chemical Society, 14 квітня 2022. http://dx.doi.org/10.1021/jacs.2c00452.
Повний текст джерелаRai, Rishika, and Kana M. Sureshan. "Topochemical Synthesis of a Heterochiral Peptide Polymer in Different Polymorphic Forms from Crystals and Aerogels." Angewandte Chemie International Edition 61, no. 16 (February 23, 2022). http://dx.doi.org/10.1002/anie.202111623.
Повний текст джерелаRai, Rishika, and Kana M. Sureshan. "Topochemical Synthesis of a Heterochiral Peptide Polymer in Different Polymorphic Forms from Crystals and Aerogels." Angewandte Chemie 134, no. 16 (February 23, 2022). http://dx.doi.org/10.1002/ange.202111623.
Повний текст джерелаRahman, Md Wazedur, Mari C. Mañas-Torres, Seyedamin Firouzeh, Sara Illescas-Lopez, Juan Manuel Cuerva, Modesto T. Lopez-Lopez, Luis Álvarez de Cienfuegos, and Sandipan Pramanik. "Chirality-Induced Spin Selectivity in Heterochiral Short-Peptide–Carbon-Nanotube Hybrid Networks: Role of Supramolecular Chirality." ACS Nano, October 11, 2022. http://dx.doi.org/10.1021/acsnano.2c07040.
Повний текст джерелаTeng, Peng, Mengmeng Zheng, Darrell Cole Cerrato, Yan Shi, Mi Zhou, Songyi Xue, Wei Jiang та ін. "The folding propensity of α/sulfono-γ-AA peptidic foldamers with both left- and right-handedness". Communications Chemistry 4, № 1 (10 травня 2021). http://dx.doi.org/10.1038/s42004-021-00496-0.
Повний текст джерелаYang, Xuejiao, Honglei Lu, Yinghua Tao, Hongyue Zhang, and Huaimin Wang. "Controlling supramolecular filament chirality of hydrogel by co-assembly of enantiomeric aromatic peptides." Journal of Nanobiotechnology 20, no. 1 (February 10, 2022). http://dx.doi.org/10.1186/s12951-022-01285-0.
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