Zn(II) binding to pramlintide results in a structural kink, fibril formation and antifungal activity.

Dudek D, Dzień E, Wątły J, Matera-Witkiewicz A, Mikołajczyk A, Hajda A, Olesiak-Bańska J, Rowińska-Żyrek M

Scientific reports29 Nov 2022Cited by 10 (Europe PMC)

PMID36446825PMCIDPMC9708664DOI10.1038/s41598-022-24968-yPepBankPUB-36446825

Summary

The antimicrobial properties of amylin, a 37-amino acid peptide hormone, co-secreted with insulin from the pancreas, are far less known than its antidiabetic function. We provide insight into the bioinorganic chemistry of amylin analogues, showing that the coordination of zinc(II) enhances the antifungal properties of pramlintide, a non-fibrillating therapeutic analogue of amylin. Zinc binds to the N-terminal amino group and His18 imidazole, inducing a kink in the peptide structure, which, in turn, triggers a fibrillization process of the complex, resulting in an amyloid structure most likely responsible for the disruption of the fungal cell.

CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study4

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone4

In this study, Pramlintide (Symlin) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Pramlintide (Symlin).

01LabNot a test of Pramlintide (Symlin) aloneIn vitro (cells)Activity measurement
In laboratory studies, zinc coordination enhanced the antifungal properties of pramlintide.
In plain wordsIn lab tests, zinc binding increased pramlintide's antifungal properties.
Peptide
Pramlintide (Symlin)
Outcome
IncreaseAntifungal properties
Study
n: not reported in source
Outcome group
Infection and antimicrobial activity · Infection
Source sentences
Summary
We provide insight into the bioinorganic chemistry of amylin analogues, showing that the coordination of zinc(II) enhances the antifungal properties of pramlintide, a non-fibrillating therapeutic analogue of amylin.
In this study, Pramlintide (Symlin) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Pramlintide (Symlin).
Show in the study text Report a problemFND-3644682501
02LabNot a test of Pramlintide (Symlin) aloneIn vitro (cells)Mechanism
In laboratory studies, the amyloid structure of zinc-complexed pramlintide likely mediated fungal cell disruption.
In plain wordsIn lab tests, the zinc-pramlintide amyloid structure likely disrupted fungal cells.
Peptide
Pramlintide (Symlin)
Outcome
Not applicableFungal cell disruption mechanism
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Infection
Source sentences
Summary
Zinc binds to the N-terminal amino group and His18 imidazole, inducing a kink in the peptide structure, which, in turn, triggers a fibrillization process of the complex, resulting in an amyloid structure most likely responsible for the disruption of the fungal cell.
In this study, Pramlintide (Symlin) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Pramlintide (Symlin).
Show in the study text Report a problemFND-3644682504
03LabNot a test of Pramlintide (Symlin) aloneIn vitro (cell-free)Mechanism
In molecular studies, zinc bound the pramlintide N-terminal amino group and His18 imidazole and induced a structural kink.
In plain wordsIn lab tests, zinc bound pramlintide and induced a bend in its structure.
Peptide
Pramlintide (Symlin)
Outcome
Not applicableZinc binding and structural kink
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Zinc binds to the N-terminal amino group and His18 imidazole, inducing a kink in the peptide structure, which, in turn, triggers a fibrillization process of the complex, resulting in an amyloid structure most likely responsible for the disruption of the fungal cell.
In this study, Pramlintide (Symlin) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Pramlintide (Symlin).
Show in the study text Report a problemFND-3644682502
04LabNot a test of Pramlintide (Symlin) aloneIn vitro (cell-free)Mechanism
In molecular studies, zinc-induced structural changes triggered fibrillization of the pramlintide complex into an amyloid structure.
In plain wordsIn lab tests, zinc binding triggered pramlintide complex formation into amyloid fibers.
Peptide
Pramlintide (Symlin)
Outcome
IncreaseFibrillization
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Zinc binds to the N-terminal amino group and His18 imidazole, inducing a kink in the peptide structure, which, in turn, triggers a fibrillization process of the complex, resulting in an amyloid structure most likely responsible for the disruption of the fungal cell.
In this study, Pramlintide (Symlin) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Pramlintide (Symlin).
Show in the study text Report a problemFND-3644682503

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

Version 2Current
22 Oct 2026, 02:26 UTC
Study results updated
Version 1
21 Oct 2026, 18:59 UTC
First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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MeSH terms

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