A minireview on the perturbation effects of polar groups to direct nanoscale hydrophobic interaction and amphiphilic peptide assembly-Reference-Cited by-同舟云学术

A minireview on the perturbation effects of polar groups to direct nanoscale hydrophobic interaction and amphiphilic peptide assembly

Published:2021 Issue:46 Volume:11 Page:28667-28673
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Zhang Feiyi¹,Yu Lanlan²,Zhang Wenbo²,Liu Lei¹^ORCID,Wang Chenxuan²^ORCID

Affiliation:

1. Institute for Advanced Materials, Jiangsu University, Zhenjiang, Jiangsu 212013, China

2. State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences Chinese Academy of Medical Sciences, School of Basic Medicine Peking Union Medical College, Beijing 100005, China

Abstract

Hydrophobic interaction provides the essential driving force for creating diverse native and artificial supramolecular architectures.

Funder

China Postdoctoral Science Foundation

National Natural Science Foundation of China

Fundamental Research Funds for the Central Universities

Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/RA/D1RA05463E

Reference50 articles.

1. Sitting at the Edge: How Biomolecules use Hydrophobicity to Tune Their Interactions and Function

2. Rationally Designed Protein Building Blocks for Programmable Hierarchical Architectures

3. Role of molecular architecture in the modulation of hydrophobic interactions

4. Thermally Triggered Self-Assembly of Folded Proteins into Vesicles

5. Hydrophobic interactions in context

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