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.

Základní údaje

Originální název

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

Autoři

TAYLOR, C., N. SCHONBERGER, Alice LANÍKOVÁ (203 Česká republika, domácí), M. PATZSCHKE, B. DROBOT, Lukáš ŽÍDEK (203 Česká republika, garant, domácí) a F. LEDERER

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.945

Kód RIV

RIV/00216224:14740/21:00121617

Organizační jednotka

Středoevropský technologický institut

DOI

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

UT WoS

000633047800001

Klíčová slova anglicky

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

Štítky

CF NMR

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 10. 2024 14:26, Ing. Jana Kuchtová

Anotace

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.

Návaznosti

871037, interní kód MU

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

Investor: Evropská unie, iNEXT-Discovery: Infrastructure for transnational access and discovery in integrated structural biology, RI Research Infrastructures (Excellent Science)

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

TAYLOR, C., N. SCHONBERGER, Alice LANÍKOVÁ, M. PATZSCHKE, B. DROBOT, Lukáš ŽÍDEK a 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, roč. 23, č. 14, s. 8618-8632. ISSN 1463-9076. Dostupné z: 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 a 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, roč.~23, č.~14, s.~8618-8632. ISSN~1463-9076. Dostupné z: https://dx.doi.org/10.1039/d1cp00356a.

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