Show simple item record

dc.contributor.authorPerry, Samuel
dc.contributor.authorHill, Timothy
dc.contributor.authorDantas de Araujo, Aline
dc.contributor.authorHoang, Huy
dc.contributor.authorFairlie, David
dc.date.accessioned2019-05-29T12:43:01Z
dc.date.available2019-05-29T12:43:01Z
dc.date.issued2018
dc.identifier.issn1477-0520
dc.identifier.doi10.1039/c7ob02952g
dc.identifier.urihttp://hdl.handle.net/10072/370484
dc.description.abstractMost protein–protein interactions occur inside cells. Peptides can inhibit protein–protein interactions but tend not to enter cells. We systematically compare cell permeability for 8–12 residue model peptides with helix-inducing lactam/hydrocarbon linkers between amino acid sidechains. Cell uptake increases when hydrophobic residues and lactam linkers (i, i + 4) form a contiguous hydrophobic surface patch. Uptake increases further when both hydrophobic and positively charged (but not neutral or negative) residues are clustered into like surface patches. Amphipathicity alone is however insufficient for cell uptake of acyclic sequences. Changing the linker from lactam to hydrocarbon further increases uptake, but also promotes cell lysis. Helicity, positive charge and amphipathicity together promote cell permeability. Most known bioactive helical peptides do not optimally cluster residues for amphipathicity and so are likely unoptimised for cell uptake.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherRoyal Society of Chemistry
dc.publisher.placeUnited Kingdom
dc.relation.ispartofpagefrom367
dc.relation.ispartofpageto371
dc.relation.ispartofissue3
dc.relation.ispartofjournalOrganic & Biomolecular Chemistry
dc.relation.ispartofvolume16
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry not elsewhere classified
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchOrganic Chemistry
dc.subject.fieldofresearchcode030499
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0305
dc.titleContiguous hydrophobic and charged surface patches in short helix-constrained peptides drive cell permeability
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorPerry, Samuel


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record