Self-assembly of penta-selenopeptides into amyloid fibrils

Abstract

Here, we report the synthesis of a penta-selenopeptide consisting of five benzyl protected selenocysteine residues. This selenopeptide was well characterized by both one- and two-dimensional (D) NMR spectroscopies. We find that the solution conformation is enriched with β-sheet structures, which have a propensity to self-assemble and form amyloid fibrils.

Self-Assembly of Nicotinic Acid-Conjugated Selenopeptides into Mesotubes

“…The existing literature on diverse kinds of intra- and intermolecular interactions with Se atom − along with the necessity of both N and Se atoms indicates that Se···N interactions or the conformational changes induced by the Se and N atoms in the dipeptide 1 are likely to morph the supramolecular assembly into a mesotubular structure. It is relevant to mention that it still remains unclear as to why certain selenopeptides form nanoscale amyloid fibrillar assemblies, while peptide 1 (or 3) assembles into a much larger, mesoscale tubular (or rodlike) architecture.…”

“…It should be emphasized that there is a lack of literature on the structural studies of selenopeptides, mainly using nuclear magnetic resonance (NMR) spectroscopy, which further limits the exploration of various morphological and biomimetic studies. , Moreover, whether selenopeptides can indeed form any specific, organized nanostructures such as tubes, fibers, rods, and spheres are barely reported in the literature. We have recently reported the synthesis of a new class of small homoselenopeptides, which tend to self-assemble in acetonitrile …”

“…We have recently reported the synthesis of a new class of small homoselenopeptides, which tend to self-assemble in acetonitrile. 32 Peptide bioconjugates, a class of compounds that combine peptides with other biomolecules, provide a platform to develop new biomaterials. 33,34 Such conjugates specifically and uniquely improve the activity of biomolecules due to their biofunctionality, biodegradability, and biocompatibility.…”

Synthesis and Self‐Assembly of Amphiphilic Ferrocene‐Selenopeptide Conjugates

“…[18][19][20][21] Self-assembly of synthetic peptides leads to a broad range of functional materials with several biomedical and biomimetic applications like in nanomedicine, drug delivery, microbial defence, structural support, and various biochemical reactions. [22][23][24][25][26] The control over the morphology of selfassembled amphiphiles obtained by varying physiochemical conditions explained the biocompatibility of peptide which makes it a suitable candidate for prospective applications in biomedicine, drug delivery, and transport. [27] Gazit and coworkers have reported the formation of diverse assembly of soft materials by coupling phenylalanine (Phe) residues, which are subsequently used in different catalytic reactions, pathological applications, and casting metal wires.…”