Evidence map›Paper›PMID 27027248›Full record

ArticleChemMedChem2016

Solution Structure and Constrained Molecular Dynamics Study of Vitamin B12 Conjugates of the Anorectic Peptide PYY(3-36).

Kelly E Henry, Deborah J Kerwood, Damian G Allis, Jayme L Workinger, Ron L Bonaccorso, George G Holz, Christian L Roth, Jon Zubieta, Robert P Doyle

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ChemMedChem, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.2field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. The role of PYY in improving insulin resistance.Frontiers in endocrinology · 2026
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Kelly E HenryDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Deborah J KerwoodDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Damian G AllisDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Jayme L WorkingerDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Ron L BonaccorsoDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
George G HolzDepartment of Medicine and Pharmacology, Institute for Human Performance, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY, 13210, USA.
Christian L RothDepartment of Pediatrics, University of Washington, Division of Endocrinology and Diabetes, Seattle Children's Research Institute, Center for Integrative Brain Research, 1900 Ninth Avenue, Seattle, WA, 98101, USA.
Jon ZubietaDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Robert P DoyleDepartment of Chemistry, Center for Science and Technology, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA. rpdoyle@syr.edu.ORCID 0000-0001-6786-5656
Syracuse University · USSUNY Upstate Medical University · USAllen Institute for Brain Science · US

Funding

Molecular Basis of Antidiabetogenic Hormone ActionR01DK069575 · NIDDK · UPSTATE MEDICAL UNIVERSITY · PI HOLZ, GEORGE G · 2007 to 2017
$2.9M
Testing Oral Delivery of the Appetite Suppressing Peptide PYY3-36 Through the VitR15DK097675 · NIDDK · SYRACUSE UNIVERSITY · PI DOYLE, ROBERT P · 2013 to 2013
$221k
NIDDK NIH HHS R01 DK069575NIDDK NIH HHS R15 DK097675
6 · The paper itself

Abstract

Vitamin B12 -peptide conjugates have considerable therapeutic potential through improved pharmacokinetic and/or pharmacodynamic properties imparted on the peptide upon covalent attachment to vitamin B12 (B12 ). There remains a lack of structural studies investigating the effects of B12 conjugation on peptide secondary structure. Determining the solution structure of a B12 -peptide conjugate or conjugates and measuring functions of the conjugate(s) at the target peptide receptor may offer considerable insight concerning the future design of fully optimized conjugates. This methodology is especially useful in tandem with constrained molecular dynamics (MD) studies, such that predictions may be made about conjugates not yet synthesized. Focusing on two B12 conjugates of the anorectic peptide PYY(3-36), one of which was previously demonstrated to have improved food intake reduction compared with PYY(3-36), we performed NMR structural analyses and used the information to conduct MD simulations. The study provides rare structural insight into vitamin B12 conjugates and validates the fact that B12 can be conjugated to a peptide without markedly affecting peptide secondary structure.

Indexed as

Binding SitesCycloaddition ReactionFluorescence Resonance Energy TransferHEK293 CellsHumansHydrogen BondingMagnetic Resonance SpectroscopyMolecular Dynamics SimulationPeptide YYProtein Structure, TertiarySolutionsVitamin B 12Peptide YYSolutionsVitamin B 12GPCRmolecular dynamicsNMR spectroscopyPYY(3-36)vitamin B12

Identifiers

PMID27027248
PMCPMC4878914
OpenAlexW2326577490

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.