Investigation of the structure and dynamics of gallium binding
to high-affinity peptides elucidated by multi-scale simulation,
quantum chemistry, NMR and ITC dagger

J 2021

Investigation of the structure and dynamics of gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC dagger

TAYLOR, C., N. SCHONBERGER, Alice LANÍKOVÁ, M. PATZSCHKE, B. DROBOT et. al.

Basic information

Original name

Investigation of the structure and dynamics of gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC dagger

Authors

TAYLOR, C., N. SCHONBERGER, Alice LANÍKOVÁ (203 Czech Republic, belonging to the institution), M. PATZSCHKE, B. DROBOT, Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution) and F. LEDERER

Edition

Physical Chemistry Chemical Physics, CAMBRIDGE, Royal Society of Chemistry, 2021, 1463-9076

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10403 Physical chemistry

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.945

RIV identification code

RIV/00216224:14740/21:00121617

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1039/d1cp00356a

UT WoS

000633047800001

Keywords in English

high-affinity peptides; multi-scale simulation; quantum chemistry; NMR; ITC

Abstract

V originále

Gallium (as Ga3+) is a Group IIIa metal and its recovery from wastewaters has become increasingly important for its reuse. The use of peptides for recycling offers a low-cost and environmentally-friendly option but the structural characteristics of peptides likely to bind Ga3+ are largely unknown. Multiple computational methods, coupled with experimental verification via NMR and Isothermal Calorimetry (ITC), were used to establish that Ga3+ binds with high affinity to peptide sequences and to elucidate the structural characteristics that contributed. It was demonstrated that peptide pre-organisation is key to Ga3+ binding and that a favourable binding position is necessarily governed by the size and shape of the electrostatic environment as much as individual electrostatic interactions with peptide residues themselves. Given favourable conditions, Ga3+ retrieved plausible binding positions involving both charged and uncharged residues that greatly increases the range of bonding possibilities with other peptide sequences and offers insights for binding other metals. The addition of pH buffer substantially improved the affinity of Ga3+ and a structural role for a buffer component was demonstrated.

Links

871037, interní kód MU

Name: iNEXT-Discovery: Infrastructure for transnational access and discovery in integrated structural biology (Acronym: iNEXT- Discovery)

Investor: European Union, RI Research Infrastructures (Excellent Science)

90127, large research infrastructures

Name: CIISB II

Citovat

TAYLOR, C., N. SCHONBERGER, Alice LANÍKOVÁ, M. PATZSCHKE, B. DROBOT, Lukáš ŽÍDEK and F. LEDERER. Investigation of the structure and dynamics of gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC dagger. Physical Chemistry Chemical Physics. CAMBRIDGE: Royal Society of Chemistry, 2021, vol. 23, No 14, p. 8618-8632. ISSN 1463-9076. Available from: https://dx.doi.org/10.1039/d1cp00356a.

@article{1769960,
   author = {Taylor, C. and Schonberger, N. and Laníková, Alice and Patzschke, M. and Drobot, B. and Žídek, Lukáš and Lederer, F.},
   article_location = {CAMBRIDGE},
   article_number = {14},
   doi = {http://dx.doi.org/10.1039/d1cp00356a},
   keywords = {high-affinity peptides; multi-scale simulation; quantum chemistry; NMR; ITC},
   language = {eng},
   issn = {1463-9076},
   journal = {Physical Chemistry Chemical Physics},
   title = {Investigation of the structure and dynamics of gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC dagger},
   url = {https://pubs.rsc.org/en/content/articlelanding/2021/CP/D1CP00356A#!divAbstract},
   volume = {23},
   year = {2021}
}

TY  - JOUR
ID  - 1769960
AU  - Taylor, C. - Schonberger, N. - Laníková, Alice - Patzschke, M. - Drobot, B. - Žídek, Lukáš - Lederer, F.
PY  - 2021
TI  - Investigation of the structure and dynamics of gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC dagger
JF  - Physical Chemistry Chemical Physics
VL  - 23
IS  - 14
SP  - 8618-8632
EP  - 8618-8632
PB  - Royal Society of Chemistry
SN  - 14639076
KW  - high-affinity peptides
KW  - multi-scale simulation
KW  - quantum chemistry
KW  - NMR
KW  - ITC
UR  - https://pubs.rsc.org/en/content/articlelanding/2021/CP/D1CP00356A#!divAbstract
N2  - Gallium (as Ga3+) is a Group IIIa metal and its recovery from wastewaters has become increasingly important for its reuse. The use of peptides for recycling offers a low-cost and environmentally-friendly option but the structural characteristics of peptides likely to bind Ga3+ are largely unknown. Multiple computational methods, coupled with experimental verification via NMR and Isothermal Calorimetry (ITC), were used to establish that Ga3+ binds with high affinity to peptide sequences and to elucidate the structural characteristics that contributed. It was demonstrated that peptide pre-organisation is key to Ga3+ binding and that a favourable binding position is necessarily governed by the size and shape of the electrostatic environment as much as individual electrostatic interactions with peptide residues themselves. Given favourable conditions, Ga3+ retrieved plausible binding positions involving both charged and uncharged residues that greatly increases the range of bonding possibilities with other peptide sequences and offers insights for binding other metals. The addition of pH buffer substantially improved the affinity of Ga3+ and a structural role for a buffer component was demonstrated.
ER  -

TAYLOR, C., N. SCHONBERGER, Alice LANÍKOVÁ, M. PATZSCHKE, B. DROBOT, Lukáš ŽÍDEK and F. LEDERER. Investigation of the structure and dynamics of gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC dagger. \textit{Physical Chemistry Chemical Physics}. CAMBRIDGE: Royal Society of Chemistry, 2021, vol.~23, No~14, p.~8618-8632. ISSN~1463-9076. Available from: https://dx.doi.org/10.1039/d1cp00356a.

Detailed Information on Publication Record