Synthetic pores that selectively transport ions of biological significance through membranes could be potentially used in medical diagnostics or therapeutics. Herein, we report cation-selective octapeptide pores derived from alanine and aminopicolinic acid. The ion transport mechanism through the pores has been established to be a cation-chloride symport. The cation-chloride co-transport is biologically essential for the efficient functioning of the central nervous system and has been implicated in diseases such as epilepsy. The pores formed in synthetic lipid bilayers do not exhibit any closing events. The ease of synthesis as well as infinite lifetimes of these pores provides scope for modifying their transport behaviour to develop sensors. © The Royal Society of Chemistry 2016.

Amal Kanti Bera

Department Of Biotechnology

Debajyoti Basak

Sucheta Sridhar

Amino acids

Chlorine compounds

Diagnosis

Lipid bilayers

Neurology

BIOLOGICAL SIGNIFICANCE

CENTRAL NERVOUS SYSTEMS

ION TRANSPORT MECHANISMS

Medical diagnostics

OCTAPEPTIDE

SYMPORTS

SYNTHETIC LIPID

Transport behaviour

Positive ions

3-AMINOPICOLINIC ACID

chloride

oligopeptide

picolinic acid derivative

chemistry

Porosity

Chlorides

Oligopeptides

Picolinic Acids

Fulltext

IIT Madras is a public technical and research university located in Chennai, Tamil Nadu. Founded in 1959, it is recognised as an Institute of National Importance.

IIT Madras has been ranked as the top engineering institute in India for four years in a row by the National Institutional Ranking Framework of the MHRD

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IIT Madras

Organic and Biomolecular Chemistry

Synthetic channels or pores that are easy to synthesize, stable and cation-selective are extremely attractive for the development of therapeutics and materials. Herein, we report a pore developed from a small tetrapeptide scaffold that shows a preference for sodium over lithium/potassium. The sodium selectivity is attributed to the appended oligoether tail at the C-terminus. A peptide dimer is proposed as the predominant cation-transporting pore. Such pyridine containing stable pores can be potentially utilized for the pH modulated ion transport. © 2017 Elsevier Ltd

Bioorganic and Medicinal Chemistry Letters

A minimalistic tetrapeptide amphiphile scaffold for transmembrane pores with a preference for sodium

Protein pores that selectively transport ions across membranes are among nature's most efficient machines. The selectivity of these pores can be exploited for ion sensing and water purification. Since it is difficult to reconstitute membrane proteins in their active form for practical applications it is desirable to develop robust synthetic compounds that selectively transport ions across cell membranes. One can envision tuning the selectivity of pores by incorporating functional groups inside the pore. Readily accessible octapeptides containing (aminomethyl)benzoic acid and alanine are reported here that preferentially transport cations over halides across the lipid bilayer. Ion transport is hypothesized through pores formed by stable assemblies of the peptides. The aromatic ring(s) appear to be proximal to the pore and could be potentially utilized for functionalizing the pore interior. © 2015 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Cation-Transporting Peptides: Scaffolds for Functionalized Pores?

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Oxacalix[2]arene[2]triazine based ion-pair transporters

Advances in Colloid and Interface Science

Functional architectures based on self-assembly of bio-inspired dipeptides: Structure modulation and its photoelectronic applications

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High-throughput optical sensing of nucleic acids in a nanopore array

Cation-halide transport through peptide pores containing aminopicolinic acid

Journal	Data powered by TypesetOrganic and Biomolecular Chemistry
Publisher	Data powered by TypesetRoyal Society of Chemistry
ISSN	14770520
Open Access	Yes