@ajlinklab

Research group at Princeton in Chemical and Biological Engineering

 Princeton, NJ
princeton.edu/~ajlgroup
Joined September 2016
  • Tweets266
  • Following192
  • Followers553
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A. James Link retweeted
J. Am. Chem. Soc.@J_A_C_SJun 24
Tangled Tail of Mechanically Interlocked Peptides | Journal of the American Chemical Society pubs.acs.org/doi/10.1021/jac…

Tangled Tail of Mechanically Interlocked Peptides

Abstract. First synthesized by chemists in the 1960s, mechanically interlocked molecules (MIMs) were created out of scientific curiosity and thought only t

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A. James Link retweeted
J. Am. Chem. Soc.@J_A_C_SMar 9
Repositioning the Leader Peptide in Graspetide Biosynthesis | Journal of the American Chemical Society pubs.acs.org/doi/10.1021/jac…

Repositioning the Leader Peptide in Graspetide Biosynthesis

Abstract. Applying enzymes from unique biosynthetic pathways in a combinatorial fashion to garner new-to-nature products has been a long-standing goal of s

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Please check out our new review in Biochemistry @ACSPublications on aspartimides in RiPPs, led by Angela Zhu: doi.org/10.1021/acs.biochem.…. Happy to be part of the special issue on the chemistry and biology of peptides!

Aspartimide Modification in RiPP Natural Products

Abstract. Multiple classes of ribosomally synthesized and post-translationally modified peptides (RiPPs) are chemically modified with an enigmatic function

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Happy to share the latest Link lab paper out @ACSPublications @J_A_C_S led by @TobyJohnson144.
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We show that the leader peptide in graspetide biosynthesis can be converted into a follower peptide while still retaining the correct modifications. We use this to make hybrid graspetide-lasso peptides. Read here: doi.org/10.1021/jacs.5c21135

Repositioning the Leader Peptide in Graspetide Biosynthesis

Abstract. Applying enzymes from unique biosynthetic pathways in a combinatorial fashion to garner new-to-nature products has been a long-standing goal of s

pubs.acs.org
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A. James Link retweeted
Toby Johnson@TobyJohnson144Mar 9
Excited to share my 1st first name paper from 🐅 @ajlinklab We report the ability to rearrange #RiPP precursor peptides, expanding opportunities for engineering PTMs in vitro and in cellulo including mechanically interlocked peptides 🔗 @LindemannTrust @omenndarlingbio
J. Am. Chem. Soc.@J_A_C_SMar 9
Repositioning the Leader Peptide in Graspetide Biosynthesis | Journal of the American Chemical Society pubs.acs.org/doi/10.1021/jac…

Repositioning the Leader Peptide in Graspetide Biosynthesis

Abstract. Applying enzymes from unique biosynthetic pathways in a combinatorial fashion to garner new-to-nature products has been a long-standing goal of s

pubs.acs.org
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New work from @ZhongyueY, @ajlinklab and Yi-Lei Zhao takes a first step toward structural prediction of RiPPs: lasso peptide. nature.com/articles/s41467-0… Access the tool here: lassopred.accre.vanderbilt.e…
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Our first step toward structural prediction of RiPPs: lasso peptide. nature.com/articles/s41467-0… This tool can be accessed from here: lassopred.accre.vanderbilt.e… @VanderbiltCSB @VICB_Vanderbilt Great working together with @ajlinklab and Yi-Lei Zhao!
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The latest Link lab paper is out @ACSCentSci : doi.org/10.1021/acscentsci.5… ! In this work, led by @bsmchoi and @TobyJohnson144 we show that an ATP-grasp enzyme from #RiPP biosynthesis can be repurposed to cyclize peptides and even proteins!

Peptide and Protein Cyclization by a Promiscuous Graspetide Synthetase

Abstract. Macrocyclic peptides have drawn considerable interest as modalities for drug discovery. Graspetides are a class of ribosomally synthesized and po

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This is a fun example of how enzymes we find in curiosity-driven natural products research can turn into potentially useful biocatalysts. Congrats to all of the authors!
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Things tend to slow down in winter, but Elsa Ding and Yaoyukun Jiang from our group have engineered a 'cold-adapted' version of a mesophilic amylase. Even with a 45-degree temperature drop, we still observe 30% activity. onlinelibrary.wiley.com/doi/… @angew_chem @VanderbiltCSB

Enhancing Cold Adaptation of Bidomain Amylases by High‐Throughput Computational Engineering

This work uncovers molecular determinants of cold adaptation in bidomain amylases by combining MD simulations and biochemical assays, revealing that increased domain separation drives enhanced...

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A. James Link retweeted
Yi Tang@yitang_ucla29 Jan 2025
In a year with so little to cheer about so far, I am happy to share our manuscript on a copper-dependent halogenase. Unbelievable effort by GS Yorick Chiang and Scientist @phdmasao at @uclachem @UclaCBE . Thank you to all collaborators and @NIGMS. nature.com/articles/s41586-0…

Copper-dependent halogenase catalyses unactivated C−H bond functionalization

Nature - A halogenase enzyme uses the copper in its active site to catalyse iterative chlorinations on multiple unactivated carbon−hydrogen bonds, enabling carbon−hydrogen...

nature.com
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The latest Link lab paper is out @BiochemistryACS!: doi.org/10.1021/acs.biochem.… This work, led by Angela Zhu, focuses on the cysimiditides, a new subfamily of #RiPPs. The cysimiditides include a tetracysteine motif that coordinates a zinc ion and a single aspartimide moiety.

Cysimiditides: RiPPs with a Zn-Tetracysteine Motif and Aspartimidylation

Abstract. Aspartimidylation is a post-translational modification found in multiple families of ribosomally synthesized and post-translationally modified pe

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There are 56 predicted cysimiditides scattered around actinobacterial genomes. We originally found some cysimiditides as part of our study on imiditides, linear peptides harboring an aspartimide: doi.org/10.1021/jacs.3c03991.

Genome Mining and Discovery of Imiditides, a Family of RiPPs with a Class-Defining Aspartimide...

Abstract. Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a large and diverse class of natural products of ribosomal origin.

pubs.acs.org
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Cysimiditides: RiPPs with a Zn-tetracysteine motif and aspartimidylation biorxiv.org/cgi/content/shor… #biorxiv_biochem
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A. James Link retweeted
Piel Lab@piel_lab9 Sep 2024
Congrats to @HubrichFlorian & @sanathrajkk0 for this exciting story finally being published. Thanks for the fruitful collaboration with @chekanlab. If you are interested in the chemical space of #RiPP #biosynthetic #enyzmes and #isoprenoids, click here: sciencedirect.com/science/ar…
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Thank you for highlighting our work on the chemoenzymatic synthesis of modified lasso peptides on the covers of @J_A_C_S! 🤩 @Hartrampf_Lab @UZH_ch #peptides
J. Am. Chem. Soc.@J_A_C_S1 Jul 2024
From this week's covers: Sidechain- and backbone-modified lasso peptides were produced via a chemoenzymatic approach, offering a promising framework for designing peptide-based drugs. @UZH_Chemistry @NinaHartrampf Learn more ➡️ go.acs.org/a2g
JACS Front Cover Volume 146, Issue 25 Image depicting the article "Merging Flow Synthesis and Enzymatic Maturation to Expand the Chemical Space of Lasso Peptides"

ALT JACS Front Cover Volume 146, Issue 25 Image depicting the article "Merging Flow Synthesis and Enzymatic Maturation to Expand the Chemical Space of Lasso Peptides"

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AlphaFold can't tell you the structure of lasso peptide, a major branch of RiPPs and promising antibiotics. Xingyu wasn't happy about it and decided to create LassoPred. Build your own lasso or download a predicted one: lassopred.accre.vanderbilt.e…. DOI: 10.26434/chemrxiv-2024-q3rn0
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A. James Link retweeted
Drew Carson@DrewCarson7123 Jun 2024
Excited to be at @BostonBacteria at Boston Univ! Looking forward to some great science #BBM2024 🧫 I’m presenting poster number 104 tomorrow, come say hi!
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Our chemoenzymatic synthesis of the lasso peptide Microcin J25 is out now in @J_A_C_S! We used flow-SPPS to synthesize several sidechain- and backbone-modified precursor peptides and demonstrated their in vitro transformation. pubs.acs.org/doi/10.1021/jac… @UZH_Chemistry @Hartrampf_Lab

Merging Flow Synthesis and Enzymatic Maturation to Expand the Chemical Space of Lasso Peptides

Abstract. Many peptidic natural products, such as lasso peptides, cyclic peptides, and cyclotides, are conformationally constrained and show biological sta

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