Self-assembly of ultra-small micelles from amphiphilic lipopeptoids

Lau, King Hang Aaron; Castelletto, Valeria; Kendall, Thomas; Šefčı́k, Ján; Hamley, Ian W.; Reza, Mehedi; Ruokolainen, Janne

doi:10.1039/c6cc09888f

Cited by 33 publications

(48 citation statements)

References 30 publications

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“…A different approach was adopted in the design of amphiphilic lipopeptoids . These structures were characterized by a central domain of alternating polar (i.e., N ‐(2‐aminoethyl)glycine (Nae) or/and N ‐[2‐carboxyethyl]glycine (Nce)) and apolar (e.g., N ‐(2‐ phenylethyl)glycine (Npe)) residues (4 or 6 total), with a domain of ionizable residues at the C termini and an aliphatic palmitic acid tail at the N termini.…”

Section: Zero Dimensional Nanostructuresmentioning

confidence: 99%

Design and preparation of organic nanomaterials using self‐assembled peptoids

Battigelli

2019

Biopolymers

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The self‐assembly and self‐organization of peptoids, peptidomimetic polymers composed of N‐substituted glycine monomers, can result in a plethora of well‐defined organic nanostructures. Such classes of nanomaterials represent highly interesting functional platforms for many applications, for example, drug delivery, sensing, and catalysis. The main advantages of using self‐assembling peptoids to engineer organic nanostructures include their chemical diversity, biocompatibility, enzymatic stability, and ease of synthesis. The goal of this review is to present a comprehensive summary of the most relevant studies regarding the self‐assembling process of peptoids into zero‐, one‐, and two‐dimensional nanostructures, with a focus on their mechanism of formation and their potential applications.

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Section: Zero Dimensional Nanostructuresmentioning

confidence: 99%

Design and preparation of organic nanomaterials using self‐assembled peptoids

Battigelli

2019

Biopolymers

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“…To the best of our knowledge, the most of structural studies on biologically active peptoids have been done using liquid surface X‐ray scattering on Langmuir monolayers. However, recent works characterizing peptoid‐siRNA conjugates for liposomal delivery, and self‐assembled lipopeptoid micelles by small angle X‐ray scattering (SAXS) need to be mentioned …”

Section: Membrane‐active Peptoids: Advanced Peptide Biomimicrymentioning

confidence: 99%

Peptoid drug discovery and optimization via surface X‐ray scattering

2019

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Synthetic polymers mimicking antimicrobial peptides have drawn considerable interest as potential therapeutics. N‐substituted glycines, or peptoids, are recognized by their in vivo stability and ease of synthesis. Peptoids are thought to act primarily on the negatively charged lipids that are abundant in bacterial cell membranes. A mechanistic understanding of lipid–peptoid interaction at the molecular level will provide insights for rational design and optimization of peptoids. Here, we highlight recent studies that utilize synchrotron liquid surface X‐ray scattering to characterize the underlying peptoid interactions with bacterial and eukaryotic membranes. Cellular membranes are highly complex, and difficult to characterize at the molecular level. Model systems including Langmuir monolayers, are used in these studies to reduce system complexity. The general workflow of these systems and the corresponding data analysis techniques are presented alongside recent findings. These studies investigate the role of peptoid physicochemical characteristics on membrane activity. Specifically, the roles of cationic charge, conformational constraint via macrocyclization, and hydrophobicity are shown to correlate their membrane interactions to biological activities in vitro. These structure–activity relationships have led to new insights into the mechanism of action by peptoid antimicrobials, and suggest optimization strategies for future therapeutics based on peptoids.

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“…Hamley and coworkers studied the self‐assembly of “lipopeptoids,” namely, polypeptide amphiphiles . The high geometric and hydrophobicity head‐to‐tail asymmetries of the lipopeptoids enable the formation of micellar structures.…”

Section: Crystallization and Self‐assembly Of Polypeptoid Polymersmentioning

confidence: 99%

Recent advances in crystallization and self‐assembly of polypeptoid polymers

Zeng

Qiu

Wen

2019

Polymer Crystallization

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Poly(N‐substituted glycine)s, or polypeptoids, have attracted great interest from researchers due to their structural similarity to polypeptides. By taking advantage of relative ease of synthesis and good solubility in common solvents, polypeptoid polymers provide a versatile platform to generate peptide mimics with well‐defined chemical structures and architectures. As a class of peptidomimetic polymers, a deep understanding on the impact of side‐chain structures, main‐chain topologies, and backbone conformations with respect to the aggregation behaviors is the prerequisite for developing peptidomimetic polymers toward macromolecular and supramolecular engineering. This mini‐review highlights recent developments in the crystallization and self‐assembly of homopolymers, block copolymers, and macrocycles of polypeptoids.

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Self-assembly of ultra-small micelles from amphiphilic lipopeptoids

Cited by 33 publications

References 30 publications

Design and preparation of organic nanomaterials using self‐assembled peptoids

Design and preparation of organic nanomaterials using self‐assembled peptoids

Peptoid drug discovery and optimization via surface X‐ray scattering

Recent advances in crystallization and self‐assembly of polypeptoid polymers

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