Adsorption–Desorption Study of BSA Conjugated Silver Nanoparticles (Ag/BSA NPs) on Collagen Immobilized Substrates

Abstract

There has been a growing interest in the use of protein conjugated nanoparticles for applications in biomedical, sensing, and advanced imaging. The objective of this study was to understand the interaction of protein conjugated silver nanoparticles (Ag/BSA NPs) with biological substrate (collagen layer). The adsorption behavior of synthesized Ag/BSA NPs on collagen immobilized silanized surface was followed by UV-vis spectroscopy by initially studying the formation of collagen layer and subsequent adsorption of Ag/BSA NPs to the immobilized layer. Surface plasmon resonance (SPR) data provided the real time profile of adsorption of Ag/BSA NPs from solution onto collagen immobilized and control substrates as well as desorption of nanoparticles from the substrates. The retention of NPs to substrate is sensitive to chemistry of the underlying substrate and on the external environment. UV-vis and atomic absorption spectrometric analysis of Ag/BSA NPs desorption performed under different pH conditions showed more NPs retained at physiological pH than the acidic and basic conditions. Nanoparticles retention on collagen immobilized substrate at physiological pH could influence properties of biological interest such as circulation lifetime and biodistribution of nanoparticles in the body.

Investigation of bovine serum albumin-surfactant aggregation and its physicochemical characteristics

“…At a higher percentage of BSA, the surface tension of water continued to decrease, but not proportionately with the added amount of BSA. Native BSA is a negatively charged globular protein with its hydrophobic segments largely buried inside [31] at pH 5.0 (point of zero charge). Water molecules bind to BSA readily through polar bonds ( COO − H 2 O) at the expense of their hydrogen bonds with the surrounding water molecules, thus decreasing the cohesive forces among themselves.…”

Mapping cellular-scale internal stiffness in 3D tissues with smart material hydrogel probes

“…S2). We did observe a small and non-significant increase in expansion variability in the 100% FBS condition, likely arising from collagen interactions with supraphysiologically high concentrations of albumin present in FBS 34 . Since in vivo interstitial albumin levels are an order of magnitude lower than in this extreme case 35 , this mechanism is unlikely to impact swelling behaviour in tissues.…”

“…Free expansion ratios of non-functionalized µTAMs were not significantly altered in even 100% fetal bovine serum (FBS; Supplementary Fig. S2), which contains supraphysiologically high levels of soluble protein 34 .…”

Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: A review

“…Because BSA typically exhibits significant surface-induced spreading upon adsorption, a stable layer of the protein can be formed under a wide number of conditions in less than 1 h [135, 205, 303]. For these reasons (and its low cost), it has been extensively used as a model protein to study adsorption [68, 80, 110, 134, 137, 139, 304, 305], to aid in the suspension of CNT [306], and to block the remaining sites of surfaces after the immobilization of a biorecognition element [250, 260, 294, 307]. BSA has also been adsorbed to the surface of PMMA nanoparticles to enhance the subsequent attachment of GOx by electrostatic interactions, retaining most of the activity of the free enzyme[308, 309].…”