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

Basak, Debajyoti; Sridhar, Sucheta; Bera, Amal Kanti; Madhavan, Nandita

doi:10.1016/j.bmcl.2017.04.081

Cited by 4 publications

(10 citation statements)

References 29 publications

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“…Within each family, the members differ by the R and R’ groups at the C‐ and N‐termini, respectively. More emphasis was placed on varying the groups at the C‐terminus as earlier results obtained with peptide 1 indicated the tetrapeptide formed dimeric pores with the C‐termini at the lipid‐water interface …”

Section: Resultsmentioning

confidence: 99%

“…Peptide 1 was synthesized as reported earlier . Peptide 2 was obtained starting from dipeptide 11 [ 32] (Scheme ).…”

Section: Resultsmentioning

confidence: 99%

“…The vesicles were equilibrated with the peptides, following which NaOH was added to increase external pH by 0.6 units (Figure a). Earlier conductance studies with peptide 1 , showed that it preferentially transported cations over anions . If peptides 2–10 behaved similar to the sodium selective peptide 1 , one would envision Na + entry into the vesicles coupled with exit of H + ions (antiport) or entry of OH − (symport) as opposed to OH − /Cl − antiport.…”

Section: Resultsmentioning

confidence: 99%

“…Acyclic oligoether chains appended to steroids or a simple β‐ diketo scaffold have also been shown to enhance cation transport . Our group has developed dimeric ion channels from a picolinic acid and alanine derived tetrapeptide amphiphile 1 with a dangling diethylene glycol unit that shows Na + selectivity (Figure a) . The pendent oligoether chain was found to enhance the cation‐selectivity of these channels.…”

Section: Introductionmentioning

confidence: 99%

“… a) Sodium selective tetrapeptide reported earlier . b) The two families of tetrapeptide amphiphiles studied herein.…”

Section: Introductionmentioning

confidence: 99%

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Basic Design Elements for Tunable Cation Transport Using Picolinic‐Acid‐Incorporated Tetrapeptides

2018

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Selective transport of cations across cell membranes is essential for various biological functions in the body. Synthetic pores that mimic the selectivity of natural ion channels are attractive for development of drugs and materials. Peptides are now emerging as attractive therapeutic agents due to their biocompatibility and ready accessibility. Herein, we report a systematic study that identifies key elements to design cation‐selective channels using tetrapeptide scaffolds. The scaffolds are derived from picolinic acid and alanine. Their ion transport activity is enhanced by hydrophobic long alkyl chains at the N‐terminus. These scaffolds are exciting as cation‐selectivity can be induced as well as switched by varying the oligoether groups at the C‐terminus.

show abstract

Section: Resultsmentioning

confidence: 99%

“…Peptide 1 was synthesized as reported earlier . Peptide 2 was obtained starting from dipeptide 11 [ 32] (Scheme ).…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“… a) Sodium selective tetrapeptide reported earlier . b) The two families of tetrapeptide amphiphiles studied herein.…”

Section: Introductionmentioning

confidence: 99%

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Basic Design Elements for Tunable Cation Transport Using Picolinic‐Acid‐Incorporated Tetrapeptides

2018

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Ligand Induced Cu^II Transport Restricts Cancer and Mycobacterial Growth: Towards a Plug‐and‐Select Ion Channel Scaffold

et al. 2021

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Synthetic channels with high ion selectivity are attractive drug targets for diseases involving ion dysregulation. Achieving selective transport of divalent ions is highly challenging due their high hydration energies. A small tripeptide amphiphilic scaffold installed with a pybox ligand selectively transports Cu II ions across membranes. The peptide forms stable dimeric pores in the membrane and transports ions by a Cu 2 + /H + antiport mechanism. The ligand-induced excellent Cu II selectivity as well as high membrane permeability of the peptide is exploited to promote cancer cell death. The peptide's ability to restrict mycobacterial growth serves as seeds to evolve antibacterial strategies centred on selectively modulating ion homeostasis in pathogens. This simple peptide can potentially function as a universal, yet versatile, scaffold wherein the ion selectivity can be precisely controlled by modifying the ligand at the C terminus.

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Low Molecular Weight Di‐ to Tetrapeptide Transmembrane Cation Transporters

2020

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Low molecular weight di‐, tri‐ and tetrapeptide transmembrane ion transporters containing aminobenzoic acid and l/d alanine are reported. These short peptides transport alkali metal cations in preference to halides across the lipid bilayer most likely through a carrier mechanism. Easy access to these peptides and the ability to install diverse functional groups into the peptidic scaffold make them attractive scaffolds for therapeutic use.

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

Cited by 4 publications

References 29 publications

Basic Design Elements for Tunable Cation Transport Using Picolinic‐Acid‐Incorporated Tetrapeptides

Basic Design Elements for Tunable Cation Transport Using Picolinic‐Acid‐Incorporated Tetrapeptides

Ligand Induced Cu^II Transport Restricts Cancer and Mycobacterial Growth: Towards a Plug‐and‐Select Ion Channel Scaffold

Low Molecular Weight Di‐ to Tetrapeptide Transmembrane Cation Transporters

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

Cited by 4 publications

References 29 publications

Basic Design Elements for Tunable Cation Transport Using Picolinic‐Acid‐Incorporated Tetrapeptides

Basic Design Elements for Tunable Cation Transport Using Picolinic‐Acid‐Incorporated Tetrapeptides

Ligand Induced CuII Transport Restricts Cancer and Mycobacterial Growth: Towards a Plug‐and‐Select Ion Channel Scaffold

Low Molecular Weight Di‐ to Tetrapeptide Transmembrane Cation Transporters

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Ligand Induced Cu^II Transport Restricts Cancer and Mycobacterial Growth: Towards a Plug‐and‐Select Ion Channel Scaffold