Enhanced protein adsorption due to charge regulation

Mikael Lund; Torbjörn Åkesson; Bo Jönsson

doi:10.1021/la050607z

Enhanced protein adsorption due to charge regulation

Mikael Lund, Torbjörn Åkesson, Bo Jönsson

Computational Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

When a protein molecule approaches a charged surface, its protonation state can undergo dramatic changes due to the imposed electric potential. This has a large impact on adsorption strengths that may be enhanced by several kT. Using mesoscopic simulation techniques as well as analytical theories, we have investigated this regulation mechanism and demonstrate how it is influenced by salt concentration and solution pH. Using hisactophilin as a test case, we show how the binding to a lipid membrane is governed by small changes in pH and that this is intimately coupled to the charge regulation mechanism.

Original language	English
Pages (from-to)	8385-8388
Journal	Langmuir
Volume	21
Issue number	18
DOIs	https://doi.org/10.1021/la050607z
Publication status	Published - 2005

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)

Subject classification (UKÄ)

Theoretical Chemistry (including Computational Chemistry)

Access to Document

10.1021/la050607z

Cite this

@article{b9508064e41549dabcdc7e04a5be6620,

title = "Enhanced protein adsorption due to charge regulation",

abstract = "When a protein molecule approaches a charged surface, its protonation state can undergo dramatic changes due to the imposed electric potential. This has a large impact on adsorption strengths that may be enhanced by several kT. Using mesoscopic simulation techniques as well as analytical theories, we have investigated this regulation mechanism and demonstrate how it is influenced by salt concentration and solution pH. Using hisactophilin as a test case, we show how the binding to a lipid membrane is governed by small changes in pH and that this is intimately coupled to the charge regulation mechanism.",

author = "Mikael Lund and Torbj{\"o}rn {\AA}kesson and Bo J{\"o}nsson",

note = "The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)",

year = "2005",

doi = "10.1021/la050607z",

language = "English",

volume = "21",

pages = "8385--8388",

journal = "Langmuir",

issn = "0743-7463",

publisher = "The American Chemical Society (ACS)",

number = "18",

}

TY - JOUR

T1 - Enhanced protein adsorption due to charge regulation

AU - Lund, Mikael

AU - Åkesson, Torbjörn

AU - Jönsson, Bo

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)

PY - 2005

Y1 - 2005

N2 - When a protein molecule approaches a charged surface, its protonation state can undergo dramatic changes due to the imposed electric potential. This has a large impact on adsorption strengths that may be enhanced by several kT. Using mesoscopic simulation techniques as well as analytical theories, we have investigated this regulation mechanism and demonstrate how it is influenced by salt concentration and solution pH. Using hisactophilin as a test case, we show how the binding to a lipid membrane is governed by small changes in pH and that this is intimately coupled to the charge regulation mechanism.

AB - When a protein molecule approaches a charged surface, its protonation state can undergo dramatic changes due to the imposed electric potential. This has a large impact on adsorption strengths that may be enhanced by several kT. Using mesoscopic simulation techniques as well as analytical theories, we have investigated this regulation mechanism and demonstrate how it is influenced by salt concentration and solution pH. Using hisactophilin as a test case, we show how the binding to a lipid membrane is governed by small changes in pH and that this is intimately coupled to the charge regulation mechanism.

UR - https://www.scopus.com/pages/publications/24944550836

U2 - 10.1021/la050607z

DO - 10.1021/la050607z

M3 - Article

SN - 0743-7463

VL - 21

SP - 8385

EP - 8388

JO - Langmuir

JF - Langmuir

IS - 18

ER -

Enhanced protein adsorption due to charge regulation

Abstract

Bibliographical note

Subject classification (UKÄ)

Access to Document

Other files and links

Fingerprint

Cite this