The
role of small molecules in the preparation of metal nanomaterials
generates considerable interest in the fields from materials science
to interdisciplinary sciences. In this study, a small amino acid, l-tyrosine (Tyr), has been used as a ligand precursor for the
preparation of silver nanomaterials (AgNMs) comprising a dual system:
smaller silver nanoclusters (responsible exclusively for the photophysical
properties) and larger silver nanoparticles (responsible exclusively
for the antimicrobial properties). The luminescent properties of this
AgNM system substantiate the role played by Tyr as a capping and a
reducing agent outside the protein environment. An interesting feature
of this report is the promising antimicrobial properties of the AgNMs
against Saccharomyces cerevisiae, Candida albicans, Escherichia coli, and Bacillus cereus cell lines.
The importance of this work is that this investigation demonstrates
the combating ability of our AgNM system against pathogenic strains
(C. albicans and B.
cereus) as well. Moreover, the mechanistic aspects
of the antimicrobial activity of the AgNMs were elucidated using various
methods, such as propidium iodide staining, monitoring reactive oxygen
species generation, leakage of proteins, DNA cleavage, etc. We propose
that AgNM-mediated cytotoxicity in S. cerevisiae stems from the generation of singlet oxygen (1O2) species that create oxidative stress, disrupting the cell membrane
and thereby resulting in leakage of proteins from the cells. This
study can pave the way toward elucidating the role of a small molecule,
Tyr, in the formation of NMs and describes the use of new NMs in potential
antimicrobial applications.
The function, stability, and turnover of plasma membrane (PM) proteins are crucial for cellular homeostasis. Compared to soluble proteins, quality control of plasma membrane proteins is extremely challenging. Failure to meet the high quality control standards is detrimental to cellular and organismal health. J-domain proteins (JDPs) are among the most diverse group of chaperones that collaborate with other chaperones and protein degradation machinery to oversee cellular protein quality control (PQC). Although fragmented, the available literature from different models, including yeast, mammals, and plants, suggests that JDPs assist PM proteins with their synthesis, folding, and trafficking to their destination as well as their degradation, either through endocytic or proteasomal degradation pathways. Moreover, some JDPs interact directly with the membrane to regulate the stability and/or functionality of proteins at the PM. The deconvoluted picture emerging is that PM proteins are relayed from one JDP to another throughout their life cycle, further underscoring the versatility of the Hsp70:JDP machinery in the cell.
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