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It was reported that proteins can bind to metal nanoparticles through free amine groups or cysteine residues and via electrostatic attraction of negatively charged carboxyl or carbonyl groups, forming a coat covering the particles to prevent agglomeration, then leading to the stabilization of AuNPs [9].
It was reported that AuNPs could interact with proteins through free amine groups or cysteine residues via electrostatic attraction of negatively charged carboxyl or carbonyl groups, forming a coat covering the particles to prevent agglomeration, thus leading to the stabilization of AuNPs [9].
From the results, it was confirmed that the SLN formulation had long-term stability; this could be attributed to higher solubility of drug in the lipid matrix and due to poloxamer 188, and because of its nonionic nature it decreases the electrostatic repulsions between the particles, thus stabilizing the nanoparticles by forming a coat around their surfaces.
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Seven to ten percent (w/w) of PEI was located on bead surface forming a coating layer as observed by scanning electron microscopy.
FTIR spectroscopic study confirmed that amino acid and peptides form a coat covering the silver nanoparticles.
First, it forms a coat along the HA that helps protect the HA from degradation by hyaluronidases or free radicals (Rodriguez and Roughley, [2006]).
Most possibly, the proteins could form a coat to cover the nanoparticles and act as capping agents for silver nanoparticle formation to avert the agglomeration of the nanoparticles; therefore, the particles are stabilized[22].
The HA is synthesized in the cytosol and the growing chain is extruded directly into the extracellular environment (Hubbard et al. [2012]), where it forms a coat around the chondrocytes (Knudson et al. [1999]).
The "victimless leather" is grown out of cell lines, which when cultured, form a living layer of tissue supported by a biodegradable polymer matrix to form a coat.
The heterodimeric NEC self-assembles to form a coat with hexagonal characteristics to mediate capsid envelopment (Hagen et al. 2015).
The lysosomal membrane contains highly glycosylated proteins whose complex intralumenal carbohydrate side chains form a coat on the inner surface of the membrane.
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