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Record W2008173472 · doi:10.1210/en.2004-1481

Bifunctional Gonadotropin-Releasing Hormone Antagonist-Progesterone Analogs with Increased Efficacy and Duration of Action

2005· article· en· W2008173472 on OpenAlexaff
Karen E. Ratcliffe, Hamish M. Fraser, Robin Sellar, Jean Rivier, Robert P. Millar

Bibliographic record

VenueEndocrinology · 2005
Typearticle
Languageen
FieldMedicine
TopicHypothalamic control of reproductive hormones
Canadian institutionsQueen's University
FundersEunice Kennedy Shriver National Institute of Child Health and Human DevelopmentEli Lilly and Company
KeywordsEndocrinologyInternal medicineAntagonistGonadotropinHormone antagonistGonadotropin-releasing hormoneHormoneLuteinizing hormoneMedicineChemistryReceptor

Abstract

fetched live from OpenAlex

GnRH peptide analogs are widely used to treat diverse clinical conditions. However, they have poor oral activity and exhibit rapid metabolic clearance, thus requiring injection and depot formulation. Because steroid hormones are bound to plasma proteins, we explored the possibility of conjugating hydroxylated progesterones to GnRH analogs to reduce metabolic clearance of the peptides. Conjugation of [D-Lys6]GnRH agonist to the alpha11-hydroxyl of alpha11-hydroxyl progesterone via a hemi-succinate bridge increased the plasma half-life after iv injection in rabbits by 3.6-fold while retaining high binding affinity, thus providing proof of concept. Five GnRH antagonists were then synthesized with 21-hydroxyprogesterone conjugated via C21-hydroxyl to positions six (conjugates A and B) and position seven (conjugates C and D) of GnRH antagonists. In the fifth compound the NH2 terminus of a GnRH antagonist lacking the first two amino acids was conjugated via the C21-hydroxyl to 21-hydroxyprogesterone (conjugate E). All five analogs bound to guinea pig progesterone binding globulin with relatively high affinities (264-1020 nM). Moreover, all five conjugates retained high progestogenic activity in stimulating a progesterone-response-element-driven chloramphenicol acetyltransferase reporter gene in the T47D breast cancer cell line. Conjugation via the epsilon-amino function of D-Lys6 (conjugates A and B) produced compounds with high binding affinity for the human GnRH receptor (15 and 7 nM) comparable to that of the unconjugated GnRH antagonists (4 and 26 nM). Conjugation via the epsilon-amino function of Lys7 (conjugates C and D) or the NH2 terminus of an N-terminally truncated antagonist (conjugate E) produced compounds of low binding affinity. Conjugates A and B also exhibited high functional antagonism of GnRH stimulation of inositol phosphate production in COS-7 cells expressing the human GnRH receptor (2.6 and 16 nM) compared with the unconjugated antagonists (1.3 and 122 nM). In accordance with their poor receptor binding affinity, conjugates C, D, and E had poor functional antagonism. Preliminary dose-finding studies in female marmosets showed transitory progesterone inhibition by 0.25 mg and prolonged suppression of 12 and 17 d by 0.5- and 1.0-mg doses. Injection of conjugate A in adult male marmosets (0.5 mg sc) rapidly suppressed plasma testosterone levels, which remained suppressed for at least 3 d. In contrast, the unconjugated parent antagonist alone or with progesterone suppressed testosterone for only 8 h to 1 d. The findings demonstrate that conjugation of progesterone to GnRH antagonists conveys plasma binding and progestogenic properties and increases their efficacy and duration of action in vivo. These new GnRH antagonists show promise as therapeutic agents for hormone-dependent diseases and as contraceptives.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Observational · Consensus signal: none
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.920
Threshold uncertainty score0.541

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.022
GPT teacher head0.273
Teacher spread0.251 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designObservational
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations20
Published2005
Admission routes1
Has abstractyes

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