Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using 1H NMR and fluorescence quenching

Julia K. Keppler; Frank D. Sönnichsen; Peter Christian Lorenzen; Karin Schwarz

doi:10.1016/j.bbapap.2014.02.007

Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using ¹H NMR and fluorescence quenching

Julia K. Keppler^*, Frank D. Sönnichsen, Peter Christian Lorenzen, Karin Schwarz

^*Corresponding author for this work

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

64 Citations (Scopus)

Abstract

The structure of β-lactoglobulin (β-LG) is well characterized, but the exact location of binding sites for retinol and (-)- epigallocatechingallate (EGCG) is still a subject of controversy. Here we report that the genetic β-LG variants A, B and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface), and β-LG A with the most binding sites for EGCG, which include Tyr20, Phe151 and His59. Upon heat related unfolding, new unspecific binding sites emerge, which are comparable in number and affinity for retinol and for EGCG, and in the three genetic variants A, B and C. The findings of our study provide new insights into the use of β-LG as nanotransporter.

Original language	English
Pages (from-to)	1083-1093
Number of pages	11
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1844
Issue number	6
DOIs	https://doi.org/10.1016/j.bbapap.2014.02.007
Publication status	Published - Jun 2014
Externally published	Yes

Keywords

Epigallocatechingallate binding
Fluorescence quenching
Genetic variant
Protein heat stability
Protein-ligand interaction
Retinol binding
β-Lactoglobulin

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10.1016/j.bbapap.2014.02.007

Cite this

@article{be8ee8603a644a20852d8120d2dac549,

title = "Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using 1H NMR and fluorescence quenching",

abstract = "The structure of β-lactoglobulin (β-LG) is well characterized, but the exact location of binding sites for retinol and (-)- epigallocatechingallate (EGCG) is still a subject of controversy. Here we report that the genetic β-LG variants A, B and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface), and β-LG A with the most binding sites for EGCG, which include Tyr20, Phe151 and His59. Upon heat related unfolding, new unspecific binding sites emerge, which are comparable in number and affinity for retinol and for EGCG, and in the three genetic variants A, B and C. The findings of our study provide new insights into the use of β-LG as nanotransporter.",

keywords = "Epigallocatechingallate binding, Fluorescence quenching, Genetic variant, Protein heat stability, Protein-ligand interaction, Retinol binding, β-Lactoglobulin",

author = "Keppler, \{Julia K.\} and S{\"o}nnichsen, \{Frank D.\} and Lorenzen, \{Peter Christian\} and Karin Schwarz",

year = "2014",

month = jun,

doi = "10.1016/j.bbapap.2014.02.007",

language = "English",

volume = "1844",

pages = "1083--1093",

journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",

issn = "1570-9639",

publisher = "Elsevier",

number = "6",

}

Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using ¹H NMR and fluorescence quenching. / Keppler, Julia K.; Sönnichsen, Frank D.; Lorenzen, Peter Christian et al.
In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1844, No. 6, 06.2014, p. 1083-1093.

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

TY - JOUR

T1 - Differences in heat stability and ligand binding among β-lactoglobulin genetic variants A, B and C using 1H NMR and fluorescence quenching

AU - Keppler, Julia K.

AU - Sönnichsen, Frank D.

AU - Lorenzen, Peter Christian

AU - Schwarz, Karin

PY - 2014/6

Y1 - 2014/6

N2 - The structure of β-lactoglobulin (β-LG) is well characterized, but the exact location of binding sites for retinol and (-)- epigallocatechingallate (EGCG) is still a subject of controversy. Here we report that the genetic β-LG variants A, B and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface), and β-LG A with the most binding sites for EGCG, which include Tyr20, Phe151 and His59. Upon heat related unfolding, new unspecific binding sites emerge, which are comparable in number and affinity for retinol and for EGCG, and in the three genetic variants A, B and C. The findings of our study provide new insights into the use of β-LG as nanotransporter.

AB - The structure of β-lactoglobulin (β-LG) is well characterized, but the exact location of binding sites for retinol and (-)- epigallocatechingallate (EGCG) is still a subject of controversy. Here we report that the genetic β-LG variants A, B and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface), and β-LG A with the most binding sites for EGCG, which include Tyr20, Phe151 and His59. Upon heat related unfolding, new unspecific binding sites emerge, which are comparable in number and affinity for retinol and for EGCG, and in the three genetic variants A, B and C. The findings of our study provide new insights into the use of β-LG as nanotransporter.

KW - Epigallocatechingallate binding

KW - Fluorescence quenching

KW - Genetic variant

KW - Protein heat stability

KW - Protein-ligand interaction

KW - Retinol binding

KW - β-Lactoglobulin

U2 - 10.1016/j.bbapap.2014.02.007

DO - 10.1016/j.bbapap.2014.02.007

M3 - Article

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AN - SCOPUS:84898606059

SN - 1570-9639

VL - 1844

SP - 1083

EP - 1093

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

IS - 6