title: All-Purpose Containers? Lipid-Binding Protein - Drug Interactions.
abstract: The combined use of in vitro (19F-NMR) and in silico (molecular docking) procedures demonstrates the affinity of a number of human calycins (lipid-binding proteins from ileum, liver, heart, adipose tissue and epidermis, and retinol-binding protein from intestine) for different drugs (mainly steroids and vastatins). Comparative evaluations on the complexes outline some of the features relevant for interaction (non-polar character of the drugs; amino acids and water molecules in the protein calyx most often involved in binding). Dissociation constants (Ki) for drugs typically lie in the same range as Ki for natural ligands; in most instances (different proteins and docking conditions), vastatins are the strongest interactors, with atorvastatin ranking top in half of the cases. The affinity of some calycins for some of the vastatins is in the order of magnitude of the drug Cmax after systemic administration in humans. The possible biological implications of this feature are discussed in connection with drug delivery parameters (route of administration, binding to carrier proteins, distribution to, and accumulation in, human tissues).
authors.affiliation: Dipartimento di Chimica, via Golgi 19, I-20133 Milano, Italy.
authors.forename: Tiziana
authors.initials: T
authors.lastname: Beringhelli
authors.affiliation: Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Gruppo di Studio per la Proteomica e la Struttura delle Proteine, Sezione di Scienze Farmacologiche, via Balzaretti 9, I-20133 Milano, Italy.
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Gianazza
authors.affiliation: Dipartimento di Chimica, via Golgi 19, I-20133 Milano, Italy.
authors.forename: Daniela
authors.initials: D
authors.lastname: Maggioni
authors.affiliation: Dipartimento di Chimica, via Golgi 19, I-20133 Milano, Italy.
authors.forename: Sandra
authors.initials: S
authors.lastname: Scanu
authors.affiliation: Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Laboratorio di Biochimica e Biofisica Computazionale, Sezione di Biochimica, Biofisica, Fisiologia ed Immunopatologia, via Trentacoste, 2, I-20134 Milano, Italy.
authors.forename: Chiara
authors.initials: C
authors.lastname: Parravicini
authors.affiliation: Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Laboratorio di Biochimica e Biofisica Computazionale, Sezione di Biochimica, Biofisica, Fisiologia ed Immunopatologia, via Trentacoste, 2, I-20134 Milano, Italy.
authors.forename: Cristina
authors.initials: C
authors.lastname: Sensi
authors.affiliation: Università degli Studi di Verona, Dipartimento di Biotecnologie, Ca' Vignal 1, strada Le Grazie 15, I-37134 Verona, Italy.
authors.forename: Hugo L
authors.initials: HL
authors.lastname: Monaco
authors.affiliation: Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Laboratorio di Biochimica e Biofisica Computazionale, Sezione di Biochimica, Biofisica, Fisiologia ed Immunopatologia, via Trentacoste, 2, I-20134 Milano, Italy.
authors.forename: Ivano
authors.initials: I
authors.lastname: Eberini
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D002645:Chickens; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D016503:Drug Delivery Systems; D004347:Drug Interactions; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008024:Ligands; D008099:Liver / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D062105:Molecular Docking Simulation; D011487:Protein Conformation
chemical_list: D050556:Fatty Acid-Binding Proteins; D008024:Ligands