ABSTRACT
Magnetic nanoparticles (MNPs) have great potential in biochemistry and medical science. In particular, iron oxide nanoparticles have demonstrated a promising effect in various biomedical applications due to their high magnetic properties, large surface area, stability, and easy functionalization. However, colloidal stability, biocompatibility, and potential toxicity of MNPs in physiological environments are crucial for their in vivo application. In this context, many research articles focused on the possible procedures for MNPs coating to improve their physic-chemical and biological properties. This review highlights one viable fabrication strategy of biocompatible iron oxide nanoparticles using human serum albumin (HSA). HSA is mainly a transport protein with many functions in various fundamental processes. As it is one of the most abundant plasma proteins, not a single drug in the blood passes without its strength test. It influences the stability, pharmacokinetics, and biodistribution of different drug-delivery systems by binding or forming its protein corona on the surface. The development of albumin-based drug carriers is gaining increasing importance in the targeted delivery of cancer therapy. Considering this, HSA is a highly potential candidate for nanoparticles coating and theranostics area and can provide biocompatibility, prolonged blood circulation, and possibly resolve the drug-resistance cancer problem.
ABSTRACT
Cell entry, the fundamental step in cross-species transmission of SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2), is initiated by the recognition of the host cell angiotensin-converting enzyme-2 (ACE2) receptor by the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2. To date, several peptides have been proposed against SARS-CoV-2 both as inhibitor agents or as detection tools that can also be attached to the surfaces of nanoparticle carriers. But owing to their natural amino acid sequences, such peptides cannot be considered as efficient therapeutic candidates from a biostability point of view. This discussion demonstrates the design strategy of synthetic nonprotein amino acid substituted peptides with enhanced biostability and binding affinity, the implication of which can make those peptides potential therapeutic agents for inhibition and simple detection tools.