Deciphering the mechanism of protein interaction with silk fibroin for drug delivery systems.
Silk fibroin (SF) is an exceptional drug delivery carrier with respect to stabilizing, protecting, and delivering sensitive biologics. A synopsis of thermodynamic, static light scattering, hydrophobicity probing, and nanoparticle tracking analyses served as a basis to decipher the mechanism of interaction between SF and two model proteins, protamine and polylysine. The impact of salts aiding (chaotropic), not affecting (neutral), or opposing (cosmotropic) SF unfolding was a major determinant, ranging from complete abolishment to maximal interaction efficacy. Evidence is provided, that the underlying mechanism of the remarkable ability to tailor drug/SF interaction throughout such large ranges and by appropriate salt selection is the control of structural breakdown of SF micelles as present in pure SF ad initium. This study provides a mechanistically justified and hypothesis driven blueprint for future experimental designs addressing the controlled interaction of biologics and SF.
Institute for Pharmacy, University of Würzburg, Am Hubland, DE-97074 Würzburg, Germany.
Oliver
O
Germershaus
Institute for Pharmacy, University of Würzburg, Am Hubland, DE-97074 Würzburg, Germany.
Vera
V
Werner
Institute for Pharmacy, University of Würzburg, Am Hubland, DE-97074 Würzburg, Germany.
Marika
M
Kutscher
Institute for Pharmacy, University of Würzburg, Am Hubland, DE-97074 Würzburg, Germany. Electronic address: l.meinel@pharmazie.uni-wuerzburg.de.
Lorenz
L
Meinel
D002151:Calorimetry; D016503:Drug Delivery Systems; D005349:Fibroins / Q000378:metabolism*; D011107:Polylysine / Q000378:metabolism*; D011479:Protamines / Q000378:metabolism*; D011485:Protein Binding; D047011:Silk / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011479:Protamines; D047011:Silk; D011107:Polylysine; D005349:Fibroins
Drug delivery of biologics; Mechanism of interaction; Silk fibroin; Thermodynamics