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Table 1 Summary of structure-function analysis of adiponectin fragments

From: Design and development of a peptide-based adiponectin receptor agonist for cancer treatment

Original Peptide (aa number in adiponectin)

Cytostatic Activity of Original Peptide vs. gAd (% Increase)

Sequence Modifications of Original Peptide

Cytostatic Activity of Modified Peptides vs. gAd (% Increase)

ADP 23

(149-158)

17

Lys-Phe-His-Cys-Asn-Ile-Pro-Gly-Leu-Tyr * * # *

0-61

ADP 24

(151-160)

39

His-Cys-Asn-Ile-Pro-Gly-Leu-Tyr-Tyr-Phe # # # #

0-40

ADP 25

(153-162)

11

Asn-Ile-Pro-Gly-Leu-Tyr-Tyr-Phe-Ala-Tyr * * * *

21-126

ADP 26

(155-164)

33

Pro-Gly-Leu-Tyr-Tyr-Phe-Ala-Tyr-His-Ile # # # #

0-33

ADP 27

(157-155)

33

Leu-Tyr-Tyr-Phe-Ala-Tyr-His-Ile-Thr-Val # # * #

0-66

  1. Proposed minimal active site: Ile-Pro-Gly-Leu-Tyr-Tyr-Phe-Ala
  2. Conservative substitutions allowed (bolded): X-Ile-Pro-Gly-Leu-Tyr-Tyr-Phe-Ala-X
  3. The cytostatic activity of original and modified peptides was evaluated in MCF-7 cells, as described in Methods and was calculated relative to the activity of gAd (baseline). Underlined amino acids indicate the residues where conservative modifications were made. Replaceable residues are marked with * and non-replaceable residues are marked with #. X, non-natural amino acid.
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BMC Biotechnology

ISSN: 1472-6750

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