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‘Smart’ insulin-delivery technologies and intrinsic glucose-responsive insulin analogues

Diabetologia, 2021-05, Vol.64 (5), p.1016-1029

2021

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Diabetes-Associated Mutations in Proinsulin Provide a “Molecular Rheostat” of Nascent Foldability

Current diabetes reports, 2022-02, Vol.22 (2), p.85-94

2022

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Distinct states of proinsulin misfolding in MIDY

Cellular and molecular life sciences : CMLS, 2021-08, Vol.78 (16), p.6017-6031

2021

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Se‐Glargine: Chemical Synthesis of a Basal Insulin Analogue Stabilized by an Internal Diselenide Bridge

Chembiochem : a European journal of chemical biology, 2024-03, Vol.25 (5), p.e202300818-n/a

2024

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Structural Lessons From the Mutant Proinsulin Syndrome

Frontiers in endocrinology (Lausanne), 2021-09, Vol.12, p.754693

2021

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Reassessment of an Innovative Insulin Analogue Excludes Protracted Action yet Highlights the Distinction between External and Internal Diselenide Bridges

Chemistry : a European journal, 2020-04, Vol.26 (21), p.4695-4700

2020

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Scope and Limitations of Fmoc Chemistry SPPS‐Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin

Chemistry : a European journal, 2017-01, Vol.23 (7), p.1709-1716

2017

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Peptide Model of the Mutant Proinsulin Syndrome. II. Nascent Structure and Biological Implications

Frontiers in endocrinology (Lausanne), 2022-03, Vol.13, p.821091

2022

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Peptide Model of the Mutant Proinsulin Syndrome. I. Design and Clinical Correlation

Frontiers in endocrinology (Lausanne), 2022-03, Vol.13, p.821069

2022

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Refinement of Peptide Conformational Ensembles by 2D IR Spectroscopy: Application to Ala‒Ala‒Ala

Biophysical journal, 2018-06, Vol.114 (12), p.2820-2832

2018

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Direct observation of protein-peptide folding and binding in the formation of ribonuclease S

Biophysical journal, 2024-02, Vol.123 (3), p.461a-462a

2024

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A Chemical Counterpart to the Resolution Step of Nature’s Intein-Mediated Protein Splicing

ACS chemical biology, 2024-01, Vol.19 (1), p.9-14

2024

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Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in [alpha],[beta]2,3-Hybrid Peptides

Chemistry : a European journal, 2015-06, Vol.21 (26), p.9332

2015

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Can Helical Peptides Unwind One Turn at a Time? ‐ Controlled Conformational Transitions in α,β 2,3 ‐Hybrid Peptides

Chemistry : a European journal, 2015-06, Vol.21 (26), p.9332-9338

2015

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Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β2,3-Hybrid Peptides

Chemistry : a European journal, 2015-06, Vol.21 (26), p.9332-9338

2015

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Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in alpha , beta super(2,3)-Hybrid Peptides

Chemistry : a European journal, 2015-06, Vol.21 (26), p.9332-9338

2015

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Conformational Switching in Heterochiral [alpha],[beta]2,3-Hybrid Peptides in Response to Solvent Polarity

European journal of organic chemistry, 2015-08, Vol.2015 (24), p.5321

2015

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Conformational Switching in Heterochiral α,β2,3-Hybrid Peptides in Response to Solvent Polarity

European journal of organic chemistry, 2015-08, Vol.2015 (24), p.5321-5325

2015

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Conformational Switching in Heterochiral α,β 2,3 ‐Hybrid Peptides in Response to Solvent Polarity

European journal of organic chemistry, 2015-08, Vol.2015 (24), p.5321-5325

2015

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New Horizons: Next-Generation Insulin Analogues: Structural Principles and Clinical Goals

The journal of clinical endocrinology and metabolism, 2022-03, Vol.107 (4), p.909-928

2022

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Refining Peptide Conformational Landscape by Amide I Infrared Spectroscopy and MD Simulations

Biophysical journal, 2018-02, Vol.114 (3), p.387a-387a

2018

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Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β(2,3)-Hybrid Peptides

Chemistry : a European journal, 2015-06, Vol.21 (26), p.9332-9338

2015

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Obviation of hydrogen fluoride in Boc chemistry solid phase peptide synthesis of peptide-αthioestersElectronic supplementary information (ESI) available: LC-MS chromatograms/spectra, and supporting data tables. See DOI: 10.1039/c6cc07891e

2016-11

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Evolution of insulin at the edge of foldability and its medical implications

Proceedings of the National Academy of Sciences - PNAS, 2020-11, Vol.117 (47), p.29618-29628

2020

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Unprecedented Torsional Preferences in trans-[beta]2,3-Amino Acid Residues and Formation of 11-Helices in [alpha],[beta]2,3-Hybrid Peptides

Chemistry : a European journal, 2012-07, Vol.18 (31), p.9516

2012

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‘Smart’ insulin-delivery technologies and intrinsic glucose-responsive insulin analogues

Diabetes-Associated Mutations in Proinsulin Provide a “Molecular Rheostat” of Nascent Foldability

Distinct states of proinsulin misfolding in MIDY

Se‐Glargine: Chemical Synthesis of a Basal Insulin Analogue Stabilized by an Internal Diselenide Bridge

Structural Lessons From the Mutant Proinsulin Syndrome

Reassessment of an Innovative Insulin Analogue Excludes Protracted Action yet Highlights the Distinction between External and Internal Diselenide Bridges

Scope and Limitations of Fmoc Chemistry SPPS‐Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin

Peptide Model of the Mutant Proinsulin Syndrome. II. Nascent Structure and Biological Implications

Peptide Model of the Mutant Proinsulin Syndrome. I. Design and Clinical Correlation

Refinement of Peptide Conformational Ensembles by 2D IR Spectroscopy: Application to Ala‒Ala‒Ala

Direct observation of protein-peptide folding and binding in the formation of ribonuclease S

A Chemical Counterpart to the Resolution Step of Nature’s Intein-Mediated Protein Splicing

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in [alpha],[beta]2,3-Hybrid Peptides

Can Helical Peptides Unwind One Turn at a Time? ‐ Controlled Conformational Transitions in α,β 2,3 ‐Hybrid Peptides

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β2,3-Hybrid Peptides

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in alpha , beta super(2,3)-Hybrid Peptides

Conformational Switching in Heterochiral [alpha],[beta]2,3-Hybrid Peptides in Response to Solvent Polarity

Conformational Switching in Heterochiral α,β2,3-Hybrid Peptides in Response to Solvent Polarity

Conformational Switching in Heterochiral α,β 2,3 ‐Hybrid Peptides in Response to Solvent Polarity

New Horizons: Next-Generation Insulin Analogues: Structural Principles and Clinical Goals

Refining Peptide Conformational Landscape by Amide I Infrared Spectroscopy and MD Simulations

Can Helical Peptides Unwind One Turn at a Time? - Controlled Conformational Transitions in α,β(2,3)-Hybrid Peptides

Obviation of hydrogen fluoride in Boc chemistry solid phase peptide synthesis of peptide-αthioestersElectronic supplementary information (ESI) available: LC-MS chromatograms/spectra, and supporting data tables. See DOI: 10.1039/c6cc07891e

Evolution of insulin at the edge of foldability and its medical implications

Unprecedented Torsional Preferences in trans-[beta]2,3-Amino Acid Residues and Formation of 11-Helices in [alpha],[beta]2,3-Hybrid Peptides

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