Cyclo(Val-Val-Ile-d-Ala-Trp-Gly)

Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (compound 5) at concentrations of 10-100 μM does not inhibit Aβ1-42 fibrillation at equimolar concentrations, but exerts a weak effect when its molar amount is 10-fold higher than that of the synthetic Aβ1-42 peptide^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (0.5-10 μM; 12 h) does not inhibit the oligomerization of Aβ1-42 at sub-stoichiometric ratios, and inhibitory effects are only detected at equimolar concentrations with synthetic Aβ1-42 peptide^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (10 μM) interacts with monomeric fluorescein-labeled Aβ1-42 with low affinity^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (10 μM) shows no detectable interaction with monomeric fluorescein-labeled Aβ1-28 peptide^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (10 μM) binds to fluorescein-labeled monomeric Aβ15-36 peptide with high affinity, as evidenced by a significant reduction in intrinsic fluorescence, with an apparent K_d of 0.58 μM^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (75 μM) binds to oligomeric Aβ1-42 molecules, which is confirmed by the positive STD NMR signal observed in the presence of Aβ1-42^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (6-60 μM) does not inhibit IAPP fibrillation when used at equimolar concentrations or at a 10-fold molar excess relative to the synthetic IAPP peptide^[1].
Cyclo (Val-Val-Ile-d-Ala-Trp-Gly) (10 μM) binds to monomeric fluorescein-labeled IAPP peptide with low affinity^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.