Molecular evidence of stereo-specific lactoferrin dimers in solution.

Björn Persson; Mikael Lund; Jan Forsman; Dereck E W Chatterton; Torbjörn Åkesson

doi:10.1016/j.bpc.2010.06.005

Molecular evidence of stereo-specific lactoferrin dimers in solution.

Björn Persson, Mikael Lund, Jan Forsman, Dereck E W Chatterton, Torbjörn Åkesson

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

Abstract

Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.

Original language	English
Pages (from-to)	187-189
Journal	Biophysical Chemistry
Volume	151
Issue number	3
DOIs	https://doi.org/10.1016/j.bpc.2010.06.005
Publication status	Published - 2010

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

10.1016/j.bpc.2010.06.005

Cite this

@article{b6f094c74785468ab1334faf7acc74df,

title = "Molecular evidence of stereo-specific lactoferrin dimers in solution.",

abstract = "Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.",

author = "Bj{\"o}rn Persson and Mikael Lund and Jan Forsman and Chatterton, \{Dereck E W\} and Torbj{\"o}rn {\AA}kesson",

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 = "2010",

doi = "10.1016/j.bpc.2010.06.005",

language = "English",

volume = "151",

pages = "187--189",

journal = "Biophysical Chemistry",

issn = "1873-4200",

publisher = "Elsevier",

number = "3",

}

TY - JOUR

T1 - Molecular evidence of stereo-specific lactoferrin dimers in solution.

AU - Persson, Björn

AU - Lund, Mikael

AU - Forsman, Jan

AU - Chatterton, Dereck E W

AU - Åkesson, Torbjörn

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 - 2010

Y1 - 2010

N2 - Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.

AB - Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin.

UR - https://www.scopus.com/pages/publications/77955846507

U2 - 10.1016/j.bpc.2010.06.005

DO - 10.1016/j.bpc.2010.06.005

M3 - Article

C2 - 20674143

SN - 1873-4200

VL - 151

SP - 187

EP - 189

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 3

ER -

Molecular evidence of stereo-specific lactoferrin dimers in solution.

Abstract

Bibliographical note

Subject classification (UKÄ)

Access to Document

Other files and links

Fingerprint

Cite this