• No results found

University of Groningen Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling Deng, Jingjing

N/A
N/A
Protected

Academic year: 2021

Share "University of Groningen Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling Deng, Jingjing"

Copied!
2
0
0

Bezig met laden.... (Bekijk nu de volledige tekst)

Hele tekst

(1)

University of Groningen

Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling

Deng, Jingjing

DOI:

10.33612/diss.112973724

IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below.

Document Version

Publisher's PDF, also known as Version of record

Publication date: 2020

Link to publication in University of Groningen/UMCG research database

Citation for published version (APA):

Deng, J. (2020). Lanthipeptide engineering: non-canonical amino acids, click chemistry and ring shuffling. University of Groningen. https://doi.org/10.33612/diss.112973724

Copyright

Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).

Take-down policy

If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.

Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum.

(2)

Propositions

associated with the PhD thesis

Lanthipeptide engineering: non-canonical amino acids,

click chemistry and ring shuffling

By Jingjing Deng

1. Lantibiotics may one day be part of the antimicrobial arsenal to combat antimicrobial resistance. (This thesis)

2. NisP is a suitable and inexpensive protease for the activation of diverse heterologously expressed lantibiotics, produced with the nisin leader and the modification machinery of nisin. (Chapter 2)

3. Large-scale engineering of lanthipeptides is a promising strategy to obtain novel bioactive variants. (Chapter 3)

4. Incorporation of non-canonical amino acids into lantibiotics can dramat-ically expand their chemical and functional space and enables the design of novel lantibiotics with improved properties (e.g. stability, specificity orbioavailability). (Chapter 4)

5. The reactive groups of specific non-canonical amino acids (e.g. alkyne and azide) can serve as chemical handles for click chemistry to conjugate antimicrobial peptides with fluorophores, peptide moieties or other antimicrobial moieties. (Chapter 4 and Chapter 5)

6. Lantibiotics can be used as lead structures to create novel variants with altered properties via chemical coupling. (Chapter 5)

7. The purpose of education is to replace an empty mind with an open one. (Malcolm Forbes)

8. Covering ninety miles is still half way to a one-hundred-mile journey. (行百里者半九十) (Strategies of the warring states)

Referenties

GERELATEERDE DOCUMENTEN

Here, lanti- biotic derivatives generated from incorporating non-canonical amino acids (ncAAs) and chemical modification via click chemistry are introduced.. 2.1 Incorporation

To further compare the versatility of NisP in culture conditions with various proteases frequently used in biotechnology, we mutated the last four amino acids in the leader

Three different nisin hinge region variants, NMK (nisin wild-type), GLV (nisin hinge-variant 1) and GGC (nisin hinge-variant 2) were produced by strain L. lactis NZ9000

These mutants were used to evaluate the incorporation efficiency of the methionine analogues at the different positions and investigate the antimicrobial activity of these

Six dimeric nisin constructs, three nisin hybrids and six fluorescently labeled nisin variants were prepared by using click chemistry and their antimicrobial activity were tested.

Chapter 2 investigates the specificity and application of the lantibiotic protease NisP. Two sets of nisin variants were constructed to test the ability of NisP to cleave leaders

alkyn of azide) en voortgekomen zijn uit het werk van hoofdstuk 4,om vervolgens nisine te verbinden met peptidegroepen en fluorescerende probes. Zes dimere nisine construc- ten,

I would also like to thank all other (ex-) members of MolGen for their help and friendship.. Fleur, Victoria, Diego, Ruben, Claudia, Jhonatan, Eduardo, Anna, Barbara,