Please use this identifier to cite or link to this item: https://dspace.iiti.ac.in/handle/123456789/9293
Title: Chemical reactions directed peptide self-assembly
Authors: Das, Apurba Kumar
Keywords: acetyl coenzyme A;amide;ascorbic acid;chymotrypsin;cysteine;enzyme;nanomaterial;peptide;proteinase;selenium;thermolysin;thioester;triacylglycerol lipase;tryptophan;actin polymerization;biocompatibility;biological activity;biomineralization;biotransformation;chemical reaction;cyclization;enzyme activity;enzyme mechanism;genetic procedures;high performance liquid chromatography;ligation;macrocyclization;molecular interaction;nanofabrication;nonhuman;peptide synthesis;photochemistry;protein assembly;protein hydrolysis;Review;tissue engineering;transesterification;ultrasound;wound healing;biocatalysis;chemical phenomena;chemistry;hydrolysis;light;molecular model;synthesis;Biocatalysis;Chemical Phenomena;Hydrolysis;Light;Models, Molecular;Peptides
Issue Date: 2015
Publisher: MDPI AG
Citation: Rasale, D. B., & Das, A. K. (2015). Chemical reactions directed peptide self-assembly. International Journal of Molecular Sciences, 16(5), 10797-10820. doi:10.3390/ijms160510797
Abstract: Fabrication of self-assembled nanostructures is one of the important aspects in nanoscience and nanotechnology. The study of self-assembled soft materials remains an area of interest due to their potential applications in biomedicine. The versatile properties of soft materials can be tuned using a bottom up approach of small molecules. Peptide based self-assembly has significant impact in biology because of its unique features such as biocompatibility, straight peptide chain and the presence of different side chain functionality. These unique features explore peptides in various self-assembly process. In this review, we briefly introduce chemical reaction-mediated peptide self-assembly. Herein, we have emphasised enzymes, native chemical ligation and photochemical reactions in the exploration of peptide self-assembly. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
URI: https://doi.org/10.3390/ijms160510797
https://dspace.iiti.ac.in/handle/123456789/9293
ISSN: 1661-6596
Type of Material: Review
Appears in Collections:Department of Chemistry

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Altmetric Badge: