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Lynx Peptides

Analytical & peptide research

CJC-1295 without DAC

Position-2 modification, enzymatic stability and sample-specific identity analysis help explain the no-DAC GHRH analogue’s research context.

Research summary

Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation.

Drug testing and analysis 2010

Henninge J, Pepaj M, Hullstein I, Hemmersbach P

LC-HRMS/MS peptide identification

Mass spectrometry identified an amidated 29-residue peptide in a preparation marketed as CJC-1295. The proposed sequence arose from analysis of that particular sample. The finding demonstrates how molecular identity can be examined; it does not establish the complete sequence of every material sold under the same name.

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Potent long-acting growth hormone releasing factor analogues.

Annals of the New York Academy of Sciences 1988

Rivier J, Rivier C, Galyean R, Yamamoto G, Vale W

hGRF(1-29) analogue research

Changing the ends and selected residues of GHRH fragments altered receptor activity and resistance to degradation. One defined analogue had greater potency and longer action than the comparison peptide. These structure–activity results explain why exact modifications matter; they do not assign that analogue’s sequence to a separately labelled no-DAC preparation.

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Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.

The Journal of clinical investigation 1989

Frohman LA, Downs TR, Heimer EP, Felix AM

Cellular and animal mechanistic research

D-amino-acid substitution at position 1 or 2 protected defined GHRH preparations against cleavage by DPP-IV in plasma experiments. Native and shortened GHRH fragments were readily cleaved near the N-terminus, with additional trypsin-like degradation contributing less. This explains the interest in position-2 modifications without establishing the rest of a catalogue analogue’s sequence.

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Models studied

  • Mass-spectrometric peptide identification
  • hGRF(1-29) analogue stability
  • GRF-receptor binding
  • Growth-hormone release models

Key findings

  • Why position 2 matters

    N-terminal D-amino-acid substitutions can protect GHRH preparations from DPP-IV cleavage; that mechanism does not identify all residues of a separately sold analogue.

  • What an identity analysis establishes

    A sample-specific mass-spectrometry result illustrates identity analysis without resolving every preparation marketed under the same name.

References

  1. Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation.

    Drug testing and analysis 2010

    Henninge J, Pepaj M, Hullstein I, Hemmersbach P

    PMID 21204297

    View on PubMed

  2. Potent long-acting growth hormone releasing factor analogues.

    Annals of the New York Academy of Sciences 1988

    Rivier J, Rivier C, Galyean R, Yamamoto G, Vale W

    PMID 3133968

    View on PubMed

  3. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.

    The Journal of clinical investigation 1989

    Frohman LA, Downs TR, Heimer EP, Felix AM

    PMID 2565342

    View on PubMed

For laboratory research use only. Content is provided for research reference and is not intended as medical or veterinary guidance.