Literature DB >> 25197049

Assembly and molecular order of two-dimensional peptoid nanosheets through the oil-water interface.

Ellen J Robertson1, Gloria K Oliver2, Menglu Qian2, Caroline Proulx2, Ronald N Zuckermann3, Geraldine L Richmond4.   

Abstract

Peptoid nanosheets are a recently discovered class of 2D nanomaterial that form from the self-assembly of a sequence-specific peptoid polymer at an air-water interface. Nanosheet formation occurs first through the assembly of a peptoid monolayer and subsequent compression into a bilayer structure. These bilayer materials span hundreds of micrometers in lateral dimensions and have the potential to be used in a variety of applications, such as in molecular sensors, artificial membranes, and as catalysts. This paper reports that the oil-water interface provides another opportunity for growth of these unique and highly ordered peptoid sheets. The monolayers formed at this interface are found through surface spectroscopic measurements to be highly ordered and electrostatic interactions between the charged moieties, namely carboxylate and ammonium residues, of the peptoid are essential in the ability of these peptoids to form ordered nanosheets at the oil-water interface. Expanding the mechanism of peptoid nanosheet formation to the oil-water interface and understanding the crucial role of electrostatic interactions between peptoid residues in nanosheet formation is essential for increasing the complexity and functionality of these nanomaterials.

Entities:  

Keywords:  biomimetic polymers; liquid surfaces; peptoid assembly; protein mimetic materials; vibrational sum frequency spectroscopy

Mesh:

Substances:

Year:  2014        PMID: 25197049      PMCID: PMC4169914          DOI: 10.1073/pnas.1414843111

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  21 in total

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Journal:  ACS Nano       Date:  2013-03-26       Impact factor: 15.881

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9.  Transition from disordered aggregates to ordered lattices: kinetic control of the assembly of a computationally designed peptide.

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