ArticleBiopolymers2008
Acidic-basic properties of three alanine-based peptides containing acidic and basic side chains: comparison between theory and experiment.
Article in Biopolymers, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 22 citations in OpenAlex.
- Hybrid pH Responsive Supramolecular Polymers Through the Combination of the Ureido-Pyrimidinone Motif with β-Sheet Peptide Sequences.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Computational Prediction of the Protonation Sites of Ac-Lys-(Ala)n-Lys-NH2 Peptides through Conceptual DFT Descriptors.Molecules (Basel, Switzerland) · 2017Article
- A study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamics.The protein journal · 2014Article
- Influence of the Length of the Alanine Spacer on the Acidic-Basic Properties of the Ac-Lys-(Ala)(n)-Lys-NH(2) Peptides (n = 0, 1, 2, …, 5).Journal of solution chemistry · 2012Article
- Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal.Biopolymers · 2012Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The purpose of this work was to evaluate the effect of the nature of the ionizable end groups, and the solvent, on their acid-base properties in alanine-based peptides. Hence, the acid-base properties of three alanine-based peptides: Ac-KK-(A)(7)-KK-NH(2) (KAK), Ac-OO-(A)(7)-DD-NH(2) (OAD), Ac-KK-(A)(7)-EE-NH(2) (KAE), where A, D, E, K, and O denote alanine, aspartic acid, glutamic acid, lysine, and ornithine, respectively, were determined in water and in methanol by potentiometry. With the availability of these data, the ability of two theoretical methods to simulate pH-metric titration of those peptides was assessed: (i) the electrostatically driven Monte Carlo method with the ECEPP/3 force field and the Poisson-Boltzmann approach to compute solvation energy (EDMC/PB/pH), and (ii) the molecular dynamics method with the AMBER force field and the Generalized Born model (MD/GB/pH). For OAD and KAE, pK(a1) and pK(a2) correspond to the acidic side chains. For all three compounds in both solvents, the pK(a1) value is remarkably lower than the pK(a) of a compound modeling the respective isolated side chain, which can be explained by the influence of the electrostatic field from positively charged ornithine or lysine side chains. The experimental titration curves are reproduced well by the MD/GB/pH approach, the agreement being better if restraints derived from NMR measurements are incorporated in the conformational search. Poorer agreement is achieved by the EDMC/PB/pH method.
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