Uperin antimicrobial peptides: Structures, activity, and amyloid fibril formation

Verity Baltutis, Antonio N. Calabrese, John A. Carver, Lisandra L. Martin

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Research

3 Citations (Scopus)


Australian native anuran antimicrobial peptides from the uperin family, particularly uperin 3.5, have been investigated for their ability to form amyloid fibrils. Variants of uperin peptides with alterations in their charge, in particular the removal of positive charge, significantly affect uperin amyloid fibril-forming propensity and antimicrobial activity. Positive charge is also a major determinant on the interaction of uperin 3.5 with membranes. Molecular dynamics simulations have provided insight into the initial stages of uperin 3.5 aggregation to form amyloid fibrils. Uperin 3.5 possesses chameleon-like properties whereby it can adopt either the cross-β or the unusual cross-α amyloid fibrillar conformation, depending on solution conditions. Investigating the aggregation and antimicrobial properties of uperin peptides may assist in understanding the etiology of amyloidosis conditions such as Alzheimer's disease, and in developing therapeutics for their treatment.

Original languageEnglish
Title of host publicationAntimicrobial Peptides
Subtitle of host publicationFunction, Mechanisms of Action and Role in Health and Disease
EditorsParesh Chandra Ray
Place of PublicationNew York, NY, USA
PublisherNova Science Publishers
Number of pages30
ISBN (Electronic)9781685070823
ISBN (Print)9781685070052
Publication statusPublished - 26 Aug 2021

Publication series

NameMicrobiology Research Advances
PublisherNova Science Publishers


  • Amyloid fibril
  • Antimicrobial peptide
  • Biophysical studies
  • Molecular dynamics
  • Uperin

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