Inductive effects in amino acids and peptides:Ionization constants and tryptophan fluorescence
| Autor: | Luis A. Bagatolli, Roberto P. Stock, Jesús Lara-Popoca, Henrik Seir Thoke, Enrique Rudiño-Piñera |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Ionization constants Biophysics Ab initio Biochemistry lcsh:Biochemistry purl.org/becyt/ford/1 [https] 03 medical and health sciences 0302 clinical medicine Computational chemistry Tryptophan fluorescence Ionization Molecule Peptide bond lcsh:QD415-436 purl.org/becyt/ford/1.6 [https] lcsh:QH301-705.5 Indole test chemistry.chemical_classification Chemistry Computational model Tryptophan Inductive effects Amino acid 030104 developmental biology lcsh:Biology (General) 030220 oncology & carcinogenesis Amino acids Peptides Research Article |
| Zdroj: | Lara-Popoca, J, Thoke, H S, Stock, R P, Rudino-Pinera, E & Bagatolli, L A 2020, ' Inductive effects in amino acids and peptides : Ionization constants and tryptophan fluorescence ', Biochemistry and Biophysics Reports, vol. 24, 100802 . https://doi.org/10.1016/j.bbrep.2020.100802 CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET Biochemistry and Biophysics Reports, Vol 24, Iss, Pp 100802-(2020) Biochemistry and Biophysics Reports |
| DOI: | 10.1016/j.bbrep.2020.100802 |
| Popis: | Although inductive effects in organic compounds are known to influence chemical properties such as ionization constants, their specific contribution to the properties/behavior of amino acids and functional groups in peptides remains largely unexplored. In this study we developed a computationally economical algorithm for ab initio calculation of the magnitude of inductive effects for non-aromatic molecules. The value obtained by the algorithm is called the Inductive Index and we observed a high correlation (R2 = 0.9427) between our calculations and the pKa values of the alpha-amino groups of amino acids with non-aromatic side-chains. Using a series of modified amino acids, we also found similarly high correlations (R2 > 0.9600) between Inductive Indexes and two wholly independent chemical properties: i) the pKa values of ionizable side-chains and, ii) the fluorescence response of the indole group of tryptophan. After assessing the applicability of the method of calculation at the amino acid level, we extended our study to tryptophan-containing peptides and established that inductive contributions of neighboring side-chains are transmitted through peptide bonds. We discuss possible contributions to the study of proteins. Highlights • An algorithm for ab initio calculation of inductive effects in amino acids and peptides was developed. • The inductive index calculations correlate closely with ionization behavior. • The inductive index calculations correlate closely with tryptophan fluorescence. • Inductive effects may impact the properties of functional groups in proteins. |
| Databáze: | OpenAIRE |
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