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Metal chelation, characterized by its precise interactions with diverse functional groups, assumes a pivotal role in providing structural stability and generating reactive centers within metalloproteins and metallopeptides. This, in turn, orchestrates the architecture and functionality of various biological processes in living organisms. In our biomimetic approach inspired by the intricacies of natural metallopeptides, we have purposefully designed pyridine‐bis‐tyrosine, a concise Metallopeptide Conjugate (sMPC). Demonstrating the capacity to form complexes with various bioactive metal ions, sMPC emerges as a promising tool for advancing our understanding of metal‐binding proteins and catalyzing the development of cutting‐edge biotechnological materials and technologies. Our investigations underscore the hierarchical self‐assembly of these abridged conjugates into toroidal to vesicle nanostructures, influenced by concentration, and their susceptibility to spatial manipulation through metal ion coordination with functional groups. These biocompatible metal peptide complexes and their resultant nanomaterials present specific potential as exceptional therapeutic agents to address problems associated with metal ion deficiencies, offering a facile and low‐cost alternative to traditional metallodrugs. [ABSTRACT FROM AUTHOR]

An effortless thermoplasmonic welding of multi-shaped gold nanosheets is achieved by ordinary and simple sunlight irradiation. A light-matter interaction occurred via the nanogaps of smaller nanosheets, leading to the enhancement of the electromagnetic field and thus effectively concentrating the heat at the welding point. The sPA peptide nanostructure facilitates the nanowelding of small caged gold nanostructures. [ABSTRACT FROM AUTHOR]

Lipopeptide‐inspired lipidation of two short tripeptides, Phe‐Tyr‐β‐Ala and Tyr‐Phe‐β‐Ala leads to a pair of constitutional isomers of short peptide amphiphile (sPA). These two molecules were able to mimic lipopeptides properties and therefore could be used as potential drug delivery vehicles up to target sites. Further, these isomeric peptide amphiphiles were able to synthesize stable silver nanoparticles (AgNPs) in presence of sunlight without using any reducing agents. Interestingly, the presence of AgNPs significantly controls the secondary structures of these two isomeric sPAs and hence their self‐assembly. Therefore, such AgNPs‐sPA nanostructures are further used to develop antibacterial materials. Various microscopy and spectroscopy techniques were used to characterize these nanostructures. The antibacterial analysis demonstrated that owing to high biocompatibility and less cytotoxicity, designed sPA exhibited great potential in locally addressing bacterial infections. Thus, such a strategic design of lipidated tripeptide fragments can be tuned for potential therapeutic value for future applications. [ABSTRACT FROM AUTHOR]

In search of new antibacterial agents and therapeutic strategies, during this antibiotic resistance crises, we developed a facile and effective antibacterial nanomaterial by using di‐phenylalanine based hydrophobized short peptide amphiphile (HsPA) and AuNPs. Such peptide amphiphile functionalised nanoparticles can provide a universal platform for medicinal applications owing to their unique physicochemical properties. The nanostructures of sPA and HsPA‐AuNPs hybrids were confirmed by spectroscopic and microscopy techniques. The antibacterial activity of these nanostructures were tested against clinically relevant bacteria such as Escherichia coli and found satisfactory. The HsPA acted as a model drug (Au(III) and AuNPs) delivery agent. Therefore such stimuli responsive, HsPA‐AuNPs system may open new therapeutic paradigms for emerging the theranostics. [ABSTRACT FROM AUTHOR]

Inspired by natural metallopeptides, we have rationally designed two pyridine-conjugated short peptides. These two peptide conjugates formed a pair of constitutional isomers that helped us describe their structure–function relationship. Both the isomers consisted of an equal number of aromatic amino acid residues, but shuffling was observed in the position of two key amino acids, viz; tyrosine and phenylalanine, which brought a remarkable change in their self-assembling behavior. The presence of specific functional groups and chemical diversity in both conjugates made them very active towards metal coordination. Both the constitutional isomers adopted different pathways of self-assembly, which could be further controlled or transformed by the use of transition metal ions. Interestingly, it was observed that the metal ions could precisely control the morphology of these metallopeptide nanostructures and make them more stable. Therefore, such artificial metallopeptides possess remarkable advantages over the natural counterparts primarily due to their tailor-made chemical structures. [ABSTRACT FROM AUTHOR]