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Article: Quantitative structure-activity (affinity) relationship (QSAR) study on protonation and cationization of α-amino acids

TitleQuantitative structure-activity (affinity) relationship (QSAR) study on protonation and cationization of α-amino acids
Authors
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/jpca
Citation
Journal of Physical Chemistry A, 2006, v. 110 n. 44, p. 12348-12354 How to Cite?
AbstractA quantitative structure-activity (affinity) relationship (QSAR) study is carried out to model the proton, sodium, copper, and silver cation affinities of α-amino acids (AA). Stepping multiple linear regression (MLR), partial least squares (PLS), and artificial neural network (ANN) approaches are applied to elucidate the multiple factors affecting these affinities. The MLR and PLS models reveal that the variation in proton affinity is attributed to the highest electrophilic superdelocalizability of nitrogen (major) and the number of rotatable bonds (minor) in AA. The noncovalent interactions, especially ion-dipole interactions, are responsible for the changes in Na+ affinity. The ionization potential, dipole moment of the side chain, and degree of linearity are the properties of AA that give the best correlation with the Cu+ and Ag+ affinities. The ANN models are developed to study the relationships (linear or nonlinear) between the molecular descriptors and binding affinities. The ANN models show higher predictive power. The QSAR models are used to study the binding forms of AA (neutral vs zwitterionic) upon protonation/cationization. To our knowledge, this is the first attempt to carry out a QSAR study on protonated/cationized AA to elucidate their binding properties. In virtue of the Na+ affinity ANN model, the Na + affinities of dihydroxyphenylalanine (DOPA) were predicted. This work may pave the way for the success of applying similar approaches to peptides or proteins (with AA as the building blocks) in the future. © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/146854
ISSN
2015 Impact Factor: 2.883
2015 SCImago Journal Rankings: 1.231
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSiu, FMen_HK
dc.contributor.authorChe, CMen_HK
dc.date.accessioned2012-05-23T05:42:45Z-
dc.date.available2012-05-23T05:42:45Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal of Physical Chemistry A, 2006, v. 110 n. 44, p. 12348-12354en_HK
dc.identifier.issn1089-5639en_HK
dc.identifier.urihttp://hdl.handle.net/10722/146854-
dc.description.abstractA quantitative structure-activity (affinity) relationship (QSAR) study is carried out to model the proton, sodium, copper, and silver cation affinities of α-amino acids (AA). Stepping multiple linear regression (MLR), partial least squares (PLS), and artificial neural network (ANN) approaches are applied to elucidate the multiple factors affecting these affinities. The MLR and PLS models reveal that the variation in proton affinity is attributed to the highest electrophilic superdelocalizability of nitrogen (major) and the number of rotatable bonds (minor) in AA. The noncovalent interactions, especially ion-dipole interactions, are responsible for the changes in Na+ affinity. The ionization potential, dipole moment of the side chain, and degree of linearity are the properties of AA that give the best correlation with the Cu+ and Ag+ affinities. The ANN models are developed to study the relationships (linear or nonlinear) between the molecular descriptors and binding affinities. The ANN models show higher predictive power. The QSAR models are used to study the binding forms of AA (neutral vs zwitterionic) upon protonation/cationization. To our knowledge, this is the first attempt to carry out a QSAR study on protonated/cationized AA to elucidate their binding properties. In virtue of the Na+ affinity ANN model, the Na + affinities of dihydroxyphenylalanine (DOPA) were predicted. This work may pave the way for the success of applying similar approaches to peptides or proteins (with AA as the building blocks) in the future. © 2006 American Chemical Society.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/jpcaen_HK
dc.relation.ispartofJournal of Physical Chemistry Aen_HK
dc.titleQuantitative structure-activity (affinity) relationship (QSAR) study on protonation and cationization of α-amino acidsen_HK
dc.typeArticleen_HK
dc.identifier.emailSiu, FM:fmsiu@hku.hken_HK
dc.identifier.emailChe, CM:cmche@hku.hken_HK
dc.identifier.authoritySiu, FM=rp00776en_HK
dc.identifier.authorityChe, CM=rp00670en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jp064332nen_HK
dc.identifier.pmid17078635-
dc.identifier.scopuseid_2-s2.0-33751325490en_HK
dc.identifier.hkuros199548en_US
dc.identifier.hkuros199549-
dc.identifier.hkuros199802-
dc.identifier.hkuros128141-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33751325490&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume110en_HK
dc.identifier.issue44en_HK
dc.identifier.spage12348en_HK
dc.identifier.epage12354en_HK
dc.identifier.eissn1520-5215-
dc.identifier.isiWOS:000241729200037-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSiu, FM=6701518489en_HK
dc.identifier.scopusauthoridChe, CM=7102442791en_HK

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