Probing Adsorption Behaviors of BSA onto Chiral Surfaces of Nanoparticles. Issue 16 (24th March 2018)
- Record Type:
- Journal Article
- Title:
- Probing Adsorption Behaviors of BSA onto Chiral Surfaces of Nanoparticles. Issue 16 (24th March 2018)
- Main Title:
- Probing Adsorption Behaviors of BSA onto Chiral Surfaces of Nanoparticles
- Authors:
- Wang, Xinyi
Wang, Xiaofeng
Wang, Mingzhe
Zhang, Di
Yang, Qi
Liu, Tao
Lei, Rong
Zhu, Shuifang
Zhao, Yuliang
Chen, Chunying - Abstract:
- Abstract: Chiral properties of nanoscale materials are of importance as they dominate interactions with proteins in physiological environments; however, they have rarely been investigated. In this study, a systematic investigation is conducted for the adsorption behaviors of bovine serum albumin (BSA) onto the chiral surfaces of gold nanoparticles (AuNPs), involving multiple techniques and molecular dynamic (MD) simulation. The adsorption of BSA onto both L‐ and D‐chiral surfaces of AuNPs shows discernible differences involving thermodynamics, adsorption orientation, exposed charges, and affinity. As a powerful supplement, MD simulation provides a molecular‐level understanding of protein adsorption onto nanochiral surfaces. Salt bridge interaction is proposed as a major driving force at protein–nanochiral interface interaction. The spatial distribution features of functional groups (COO −, NH3 +, and CH3 ) of chiral molecules on the nanosurface play a key role in the formation and location of salt bridges, which determine the BSA adsorption orientation and binding strength to chiral surfaces. Sequentially, BSA corona coated on nanochiral surfaces affects their uptake by cells. The results enhance the understanding of protein corona, which are important for biological effects of nanochirality in living organisms. Abstract : A systematic investigation for the adsorption behaviors of bovine serum albumin (BSA) onto chiral surfaces of gold nanoparticles is performed enhancingAbstract: Chiral properties of nanoscale materials are of importance as they dominate interactions with proteins in physiological environments; however, they have rarely been investigated. In this study, a systematic investigation is conducted for the adsorption behaviors of bovine serum albumin (BSA) onto the chiral surfaces of gold nanoparticles (AuNPs), involving multiple techniques and molecular dynamic (MD) simulation. The adsorption of BSA onto both L‐ and D‐chiral surfaces of AuNPs shows discernible differences involving thermodynamics, adsorption orientation, exposed charges, and affinity. As a powerful supplement, MD simulation provides a molecular‐level understanding of protein adsorption onto nanochiral surfaces. Salt bridge interaction is proposed as a major driving force at protein–nanochiral interface interaction. The spatial distribution features of functional groups (COO −, NH3 +, and CH3 ) of chiral molecules on the nanosurface play a key role in the formation and location of salt bridges, which determine the BSA adsorption orientation and binding strength to chiral surfaces. Sequentially, BSA corona coated on nanochiral surfaces affects their uptake by cells. The results enhance the understanding of protein corona, which are important for biological effects of nanochirality in living organisms. Abstract : A systematic investigation for the adsorption behaviors of bovine serum albumin (BSA) onto chiral surfaces of gold nanoparticles is performed enhancing the understanding of protein corona at a molecular level. The stereoscopic configuration of chiral surfaces plays a key role in the formation of salt bridges with protein, which determines the BSA adsorption orientation and binding strength. … (more)
- Is Part Of:
- Small. Volume 14:Issue 16(2018)
- Journal:
- Small
- Issue:
- Volume 14:Issue 16(2018)
- Issue Display:
- Volume 14, Issue 16 (2018)
- Year:
- 2018
- Volume:
- 14
- Issue:
- 16
- Issue Sort Value:
- 2018-0014-0016-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2018-03-24
- Subjects:
- chiral surfaces -- molecular dynamic simulation -- nanoparticles -- protein adsorption behavior
Nanotechnology -- Periodicals
Nanoparticles -- Periodicals
Microtechnology -- Periodicals
620.5 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1613-6829 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/smll.201703982 ↗
- Languages:
- English
- ISSNs:
- 1613-6810
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8309.952000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 6409.xml