Recommendation for Clarifying FDA Policy in Evaluating “Sameness” of Higher Order Structure for Generic Peptide Therapeutics

Recognizing the approach of a dramatic expansion of peptide therapeutics reaching the marketplace in recent years, led by GLP-1 receptor agonists such as semaglutide and liraglutide, the Center for Drug Evaluation and Research (CDER) branch of the US Food and Drug Administration (FDA) issued a final guidance in 2021 that was intended to assist generic drug producers in meeting Abbreviated New Drug Application (ANDA) obligations to establish "sameness" of their active peptide drug relative to that produced by innovator companies. Research and a published report by FDA scientists on best practices followed, which promulgated the use of nuclear magnetic resonance (NMR) and principal component analysis (PCA) and established a quantitative standard by which "sameness" of higher order structure for the applicant's peptide drug could be judged. A key requirement is that drug product samples be analyzed directly and non-invasively, a condition which in practice restricts sample modification to the addition of a small amount of deuterium oxide to allow signal lock and spectral data alignment (as required for NMR analysis). In the study described herein, data are presented to illustrate that 1) relatively small differences in sample pH can cause significant shifting of certain proton resonances, 2) that such resonance shifting is readily reversible and due to the degree of protonation of specific amino acid residues (rather than reflecting differences in higher order structure), and 3) that small differences in pH variability between sample cohorts can frequently cause failure to meet the quantitative benchmark established by the agency. Methodology is presented by which drug sample pHs can be aligned with minimal impact, and a recommendation is made that minor sample pH adjustments be allowed in assessing "sameness" of peptide drug higher order structure.

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Publication Details

Journal
The AAPS Journal
Published
2024-11-25
DOI
https://doi.org/10.1208/s12248-024-00994-8
Citations
1
Primary Topic
Chemical Synthesis and Analysis
Type
article
Field-Weighted Citation Impact
0.23
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article

Recommendation for Clarifying FDA Policy in Evaluating “Sameness” of Higher Order Structure for Generic Peptide Therapeutics

Jessica A. Rogers-Crovak, Edward J. Delaney, David J. Detlefsen
1 citations
The AAPS Journal
Chemical Synthesis and Analysis
0.23
article

Recommendation for Clarifying FDA Policy in Evaluating “Sameness” of Higher Order Structure for Generic Peptide Therapeutics

Jessica A. Rogers-Crovak, Edward J. Delaney, David J. Detlefsen
article en
1 citations

Abstract

Recognizing the approach of a dramatic expansion of peptide therapeutics reaching the marketplace in recent years, led by GLP-1 receptor agonists such as semaglutide and liraglutide, the Center for Drug Evaluation and Research (CDER) branch of the US Food and Drug Administration (FDA) issued a final guidance in 2021 that was intended to assist generic drug producers in meeting Abbreviated New Drug Application (ANDA) obligations to establish "sameness" of their active peptide drug relative to that produced by innovator companies. Research and a published report by FDA scientists on best practices followed, which promulgated the use of nuclear magnetic resonance (NMR) and principal component analysis (PCA) and established a quantitative standard by which "sameness" of higher order structure for the applicant's peptide drug could be judged. A key requirement is that drug product samples be analyzed directly and non-invasively, a condition which in practice restricts sample modification to the addition of a small amount of deuterium oxide to allow signal lock and spectral data alignment (as required for NMR analysis). In the study described herein, data are presented to illustrate that 1) relatively small differences in sample pH can cause significant shifting of certain proton resonances, 2) that such resonance shifting is readily reversible and due to the degree of protonation of specific amino acid residues (rather than reflecting differences in higher order structure), and 3) that small differences in pH variability between sample cohorts can frequently cause failure to meet the quantitative benchmark established by the agency. Methodology is presented by which drug sample pHs can be aligned with minimal impact, and a recommendation is made that minor sample pH adjustments be allowed in assessing "sameness" of peptide drug higher order structure.

The AAPS JournalVol. 27(1)
Walker (United States) (US)
Openalex Percentile: Top 41%
Chemical Synthesis and Analysis
0.23
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Recommendation for Clarifying FDA Policy in Evaluating “Sameness” of Higher Order Structure for Generic Peptide Therapeutics — Jessica A. Rogers-Crovak, Edward J. Delaney, et al. · The AAPS Journal (2024) | TGRS Research Map | TGRS