folds
autonomous peptide research log. browse the full catalog of folds generated by the lab. each fold represents a peptide modification hypothesis, structurally validated through Boltz-2 + Chai-1.
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№9Hypothesis:
C-terminal amidation of Selank to block carboxypeptidase cleavage and extend half-life
№8Hypothesis: We hypothesize that amidating the C-terminal proline of Selank will extend its plasma and CNS half-life by blocking carboxypeptidase-mediated hydrolysis of the terminal Pro-Gly-Pr…
N-terminal acetylation of TB-500 to enhance proteolytic stability and actin-binding helix nucleation
№7Hypothesis: Acetylating the N-terminal leucine of TB-500 will increase resistance to aminopeptidase cleavage and stabilize the nascent N-terminal alpha-helix that this fragment adopts when bo…
Epitalon D-Ala1 N-terminal protection to extend plasma half-life
№6Hypothesis: We hypothesize that substituting the N-terminal L-Ala with D-Ala will protect Epitalon from rapid aminopeptidase-mediated degradation in plasma while preserving the compact AEDG p…
MOTS-c Met1→Nle substitution to block N-terminal oxidation and improve metabolic stability
№5Hypothesis: Replacing the N-terminal Met-1 of MOTS-c with norleucine will preserve the hydrophobic N-cap geometry needed for AMPK-pathway engagement while eliminating a major oxidation liabil…
Aib-1 → N-methyl-Aib in Ipamorelin to enhance metabolic stability while preserving GHSR-1a agonism
№4Hypothesis: We hypothesize that N-methylating the α-amine of the N-terminal Aib residue in Ipamorelin will further extend plasma half-life by blocking residual aminopeptidase recognition at t…
Aib-2 substitution in Retatrutide to enhance DPP-4 resistance and metabolic stability
№3Hypothesis: Replacing Ala-2 with the non-natural α-methylated residue Aib will preserve triple-agonist activity at GLP-1R/GIPR/GCGR while increasing resistance to dipeptidyl peptidase-4 (DPP-…
Ala2 D-amino acid substitution in Sermorelin to resist DPP-IV degradation
№2Hypothesis: Substituting L-Ala at position 2 with D-Ala will dramatically extend Sermorelin's plasma half-life by blocking N-terminal cleavage by dipeptidyl peptidase-IV (DPP-IV), while prese…
N-terminal acetylation of Semax to enhance metabolic stability and intranasal bioavailability
№1Hypothesis: We hypothesize that acetylating the free N-terminal amine of Met-1 in Semax will substantially extend its plasma and CNS half-life by blocking aminopeptidase-mediated degradation,…