Using Small Peptide Segments of Amyloid-β and Humanin to Examine their Physical Interactions.

Heyl DL, Iwaniec B, Esckilsen D, Price D, Guttikonda P, Cooper J, Lombardi J, Milletti M, Evans HG

Protein and peptide letters1 Jan 2019Cited by 9 (Europe PMC)

PMID30950343DOI10.2174/0929866526666190405122117PepBankPUB-30950343

Publisher page PubMedAsk about this study

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study6

1 result from studies that gave the peptide. No result from this study comes from people.

01LabIn vitro (cell-free)Mechanism
In cell-free assays, full-length HN and the smaller HN and Aβ peptides had different effects on regulating Aβ (1-40) aggregation kinetics.
In plain wordsIn lab tests, full-length humanin and the shorter peptides each changed how amyloid-β clumps together, in different ways.
Peptide
Humanin
Outcome
MixedRegulation of Aβ (1-40) aggregation kinetics by full-length HN
Study
n: not reported in source
Synthetic peptides in co-immunoprecipitation and binding kinetics assays
Comparator
Fragment peptides
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated
Source sentences
Summary
Moreover, HN, and the smaller HN (5-15), HN (5-15 L11S), and Aβ (17-28) peptides, had different effects on regulating Aβ (1-40) aggregation kinetics.
1 context sentence(design, population, supporting numbers)
Summary · context
Peptides corresponding to amino acid residues 5- 15 of HN, HN (5-15), HN (5-15, L11S), where Leu11 was replaced with Ser, and residues 17-28 of Aβ, Aβ (17-28), were synthesized and tested for their ability to block formation of the complex between HN and Aβ (1-40).
Report a problemFND-3095034306

Studies that did not test the peptide alone5

In this study, Humanin 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 Humanin.

02LabNot a test of Humanin aloneIn vitro (cell-free)Activity measurement
In cell-free assays, the HN fragment HN (5-15) blocked the complex between HN and Aβ (1-40) more efficiently than HN (5-15, L11S) or Aβ (17-28).
In plain wordsIn lab tests, a short humanin fragment blocked the humanin and amyloid-β complex better than two other short peptides.
Peptide
Humanin
Outcome
IncreaseBlocking of the HN-Aβ (1-40) complex by HN (5-15)
Study
n: not reported in source
Synthetic peptides in co-immunoprecipitation and binding kinetics assays
Comparator
HN (5-15, L11S) and Aβ (17-28)
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Co-immunoprecipitation and binding kinetics showed that HN (5-15) was more efficient at blocking the complex between HN and Aβ (1-40) than either HN (5-15, L11S) or Aβ (17-28).
1 context sentence(design, population, supporting numbers)
Summary · context
Peptides corresponding to amino acid residues 5- 15 of HN, HN (5-15), HN (5-15, L11S), where Leu11 was replaced with Ser, and residues 17-28 of Aβ, Aβ (17-28), were synthesized and tested for their ability to block formation of the complex between HN and Aβ (1-40).
In this study, Humanin 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 Humanin.
Report a problemFND-3095034301
03LabNot a test of Humanin aloneIn vitro (cell-free)Activity measurement
In cell-free assays, HN (5-15) bound Aβ (1-40) or full-length HN more efficiently than HN (5-15, L11S) or Aβ (17-28).
In plain wordsIn lab tests, a short humanin fragment bound amyloid-β or humanin better than two other short peptides.
Peptide
Humanin
Outcome
IncreaseBinding of HN (5-15) to Aβ (1-40) or full-length HN
Study
n: not reported in source
Synthetic peptides in co-immunoprecipitation and binding kinetics assays
Comparator
HN (5-15, L11S) and Aβ (17-28)
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Binding kinetics of these smaller peptides with either full-length HN or Aβ (1-40) showed that HN (5- 15) was able to bind either Aβ (1-40) or HN more efficiently than HN (5-15, L11S) or Aβ (17-28).
1 context sentence(design, population, supporting numbers)
Summary · context
Peptides corresponding to amino acid residues 5- 15 of HN, HN (5-15), HN (5-15, L11S), where Leu11 was replaced with Ser, and residues 17-28 of Aβ, Aβ (17-28), were synthesized and tested for their ability to block formation of the complex between HN and Aβ (1-40).
In this study, Humanin 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 Humanin.
Report a problemFND-3095034302
04LabNot a test of Humanin aloneIn vitro (cell-free)Activity measurement
In cell-free assays, HN (5-15) bound Aβ (1-40) with a weaker affinity than full-length HN.
In plain wordsIn lab tests, a short humanin fragment bound amyloid-β less strongly than full-length humanin.
Peptide
Humanin
Outcome
DecreaseBinding affinity of HN (5-15) for Aβ (1-40) versus full-length HN
Study
n: not reported in source
Synthetic peptides in co-immunoprecipitation and binding kinetics assays
Comparator
Full-length HN
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Compared to full-length HN, however, HN (5-15) bound Aβ (1-40) with a weaker affinity suggesting that while HN (5-15) binds Aβ, other residues in the full length HN peptide are necessary for maximum interactions.
1 context sentence(design, population, supporting numbers)
Summary · context
Peptides corresponding to amino acid residues 5- 15 of HN, HN (5-15), HN (5-15, L11S), where Leu11 was replaced with Ser, and residues 17-28 of Aβ, Aβ (17-28), were synthesized and tested for their ability to block formation of the complex between HN and Aβ (1-40).
In this study, Humanin 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 Humanin.
Report a problemFND-3095034303
05LabNot a test of Humanin aloneIn vitro (cell-free)Activity measurement
In cell-free assays, residue L11 was more important for interactions with Aβ (1-40) than with HN.
In plain wordsIn lab tests, one humanin amino acid, L11, mattered more for binding amyloid-β than for binding humanin.
Peptide
Humanin
Outcome
Not applicableRole of Leu11 in interactions with Aβ (1-40) and HN
Study
n: not reported in source
Synthetic peptides in co-immunoprecipitation and binding kinetics assays
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
L11 was more important for interactions with Aβ (1-40) than with HN.
1 context sentence(design, population, supporting numbers)
Summary · context
Peptides corresponding to amino acid residues 5- 15 of HN, HN (5-15), HN (5-15, L11S), where Leu11 was replaced with Ser, and residues 17-28 of Aβ, Aβ (17-28), were synthesized and tested for their ability to block formation of the complex between HN and Aβ (1-40).
In this study, Humanin 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 Humanin.
Report a problemFND-3095034304
06LabNot a test of Humanin aloneIn vitro (cell-free)Activity measurement
In cell-free assays, the Aβ (17-28) segment was relatively ineffective at binding Aβ (1-40) or HN.
In plain wordsIn lab tests, a short amyloid-β segment bound poorly to amyloid-β or humanin.
Peptide
Humanin
Outcome
No significant changeBinding of Aβ (17-28) to Aβ (1-40) or HN
Study
n: not reported in source
Synthetic peptides in co-immunoprecipitation and binding kinetics assays
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Aβ (17-28) was relatively ineffective at binding to either Aβ (1-40) or HN.
1 context sentence(design, population, supporting numbers)
Summary · context
Peptides corresponding to amino acid residues 5- 15 of HN, HN (5-15), HN (5-15, L11S), where Leu11 was replaced with Ser, and residues 17-28 of Aβ, Aβ (17-28), were synthesized and tested for their ability to block formation of the complex between HN and Aβ (1-40).
In this study, Humanin 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 Humanin.
Report a problemFND-3095034305

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
13 Oct 2026, 21:44 UTC
Study results updated
Version 1
13 Oct 2026, 16:31 UTC
First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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Keywords

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