Literature DB >> 33892308

SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly.

Deepika Mathur1, Harpreet Kaur2, Anjali Dhall3, Neelam Sharma4, Gajendra P S Raghava5.   

Abstract

Nanostructures generated by self-assembly of peptides yield nanomaterials that have many therapeutic applications, including drug delivery and biomedical engineering, due to their low cytotoxicity and higher uptake by targeted cells owing to their high affinity and specificity towards cell surface receptors. Despite the promising implications of this rapidly expanding field, there is no dedicated resource to study peptide nanostructures. This study endeavours to create a repository of short peptides, which may prove to be the best models to study ordered nanostructures formed by peptide self-assembly. SAPdb has a repertoire of 1049 entries of experimentally validated nanostructures formed by the self-assembly of small peptides. It consists of 328 tripeptides, 701 dipeptides, and 20 single amino acids with some conjugate partners. Each entry encompasses comprehensive information about the peptide, such as chemical modifications, the type of nanostructure formed, experimental conditions like pH, temperature, solvent required for the self-assembly, etc. Our analysis indicates that peptides containing aromatic amino acids favour the formation of self-assembling nanostructures. Additionally, we observed that these peptides form different nanostructures under different experimental conditions. SAPdb provides this comprehensive information in a hassle-free tabulated manner at a glance. User-friendly browsing, searching, and analysis modules have been integrated for easy data retrieval, data comparison, and examination of properties. We anticipate SAPdb to be a valuable repository for researchers engaged in the burgeoning arena of nanobiotechnology. It is freely available at https://webs.iiitd.edu.in/raghava/sapdb.
Copyright © 2021 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Database; Dipeptide; Nanostructure; Self-assembly; Tripeptide

Year:  2021        PMID: 33892308     DOI: 10.1016/j.compbiomed.2021.104391

Source DB:  PubMed          Journal:  Comput Biol Med        ISSN: 0010-4825            Impact factor:   4.589


  2 in total

1.  A GSH/CB Dual-Controlled Self-Assembled Nanomedicine for High-Efficacy Doxorubicin-Resistant Breast Cancer Therapy.

Authors:  Yang Yang; Quanfeng Zhao; Zhe Peng; Yunjiang Zhou; Miao-Miao Niu; Lin Chen
Journal:  Front Pharmacol       Date:  2022-01-14       Impact factor: 5.810

2.  Evaluating the Properties of Ginger Protease-Degraded Collagen Hydrolysate and Identifying the Cleavage Site of Ginger Protease by Using an Integrated Strategy and LC-MS Technology.

Authors:  Wei Liu; Wenning Yang; Xueyan Li; Dongying Qi; Hongjiao Chen; Huining Liu; Shuang Yu; Guopeng Wang; Yang Liu
Journal:  Molecules       Date:  2022-08-06       Impact factor: 4.927

  2 in total

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