Predicting Collagen Triple Helix Stability through Additive
Effects of Terminal Residues and Caps

J 2023

Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps

FIALA, Tomáš; Emilia P BARROS; Rahel HEEB; Sereina RINIKER; Helma WENNEMERS et al.

Základní údaje

Originální název

Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps

Autoři

FIALA, Tomáš ; Emilia P BARROS; Rahel HEEB; Sereina RINIKER a Helma WENNEMERS

Vydání

Angewandte Chemie International Edition, WEINHEIM (GERMANY), Verlag Chemie, 2023, 1433-7851

Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 16.100

Označené pro přenos do RIV

DOI

https://doi.org/10.1002/anie.202214728

Klíčová slova anglicky

Collagen; n?pi* Interaction; Peptides; Terminal Capping Group; Thermal Stability

Štítky

ne MU, ne RIV

Změněno: 17. 2. 2025 10:34, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Collagen model peptides (CMPs) consisting of proline-(2S,4R)-hydroxyproline-glycine (POG) repeats have provided a breadth of knowledge of the triple helical structure of collagen, the most abundant protein in mammals. Predictive tools for triple helix stability have, however, lagged behind since the effect of CMPs with different frames ([POG](n), [OGP](n), or [GPO](n)) and capped or uncapped termini have so far been underestimated. Here, we elucidated the impact of the frame, terminal functional group and its charge on the stability of collagen triple helices. Combined experimental and theoretical studies with frame-shifted, capped and uncapped CMPs revealed that electrostatic interactions, strand preorganization, interstrand H-bonding, and steric repulsion at the termini contribute to triple helix stability. We show that these individual contributions are additive and allow for the prediction of the melting temperatures of CMP trimers.

Citovat

FIALA, Tomáš; Emilia P BARROS; Rahel HEEB; Sereina RINIKER a Helma WENNEMERS. Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps. Angewandte Chemie International Edition. WEINHEIM (GERMANY): Verlag Chemie, 2023, roč. 62, č. 3, 10 s. ISSN 1433-7851. Dostupné z: https://doi.org/10.1002/anie.202214728.

@article{2477821,
   author = {Fiala, Tomáš and Barros, Emilia P and Heeb, Rahel and Riniker, Sereina and Wennemers, Helma},
   article_location = {WEINHEIM (GERMANY)},
   article_number = {3},
   doi = {https://doi.org/10.1002/anie.202214728},
   keywords = {Collagen; n?pi* Interaction; Peptides; Terminal Capping Group; Thermal Stability},
   issn = {1433-7851},
   journal = {Angewandte Chemie International Edition},
   note = {nevzniklo na MU},
   title = {Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps},
   volume = {62},
   year = {2023}
}

TY  - JOUR
ID  - 2477821
AU  - Fiala, Tomáš - Barros, Emilia P - Heeb, Rahel - Riniker, Sereina - Wennemers, Helma
PY  - 2023
TI  - Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps
JF  - Angewandte Chemie International Edition
VL  - 62
IS  - 3
PB  - Verlag Chemie
SN  - 14337851
N1  - nevzniklo na MU
KW  - Collagen
KW  - n?pi* Interaction
KW  - Peptides
KW  - Terminal Capping Group
KW  - Thermal Stability
N2  - Collagen model peptides (CMPs) consisting of proline-(2S,4R)-hydroxyproline-glycine (POG) repeats have provided a breadth of knowledge of the triple helical structure of collagen, the most abundant protein in mammals. Predictive tools for triple helix stability have, however, lagged behind since the effect of CMPs with different frames ([POG](n), [OGP](n), or [GPO](n)) and capped or uncapped termini have so far been underestimated. Here, we elucidated the impact of the frame, terminal functional group and its charge on the stability of collagen triple helices. Combined experimental and theoretical studies with frame-shifted, capped and uncapped CMPs revealed that electrostatic interactions, strand preorganization, interstrand H-bonding, and steric repulsion at the termini contribute to triple helix stability. We show that these individual contributions are additive and allow for the prediction of the melting temperatures of CMP trimers.
ER  -

FIALA, Tomáš; Emilia P BARROS; Rahel HEEB; Sereina RINIKER a Helma WENNEMERS. Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps. \textit{Angewandte Chemie International Edition}. WEINHEIM (GERMANY): Verlag Chemie, 2023, roč.~62, č.~3, 10 s. ISSN~1433-7851. Dostupné z: https://doi.org/10.1002/anie.202214728.

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