PhD Scientific Days 2022

Pharmaceutical Sciences II. (Poster discussion will take place in the Aula during the Coffee Break)

Synthesis of modified β-peptide foldamers

Előadó neve

Erdei, Eszter

Előadó munkahelye

Research Centre for Natural Sciences

Előadó telefonszáma

+36305611658

Előadó e-mail címe

eeszter99@gmail.com

Az előadás címe

Synthesis of modified β-peptide foldamers

Szerző(k) neve és munkahelye

Eszter Erdei
Research Centre for Natural Sciences, Institute of Materials and Environmental Chemistry, Artificial Transporters Research Group, Budapest
Semmelweis University, Faculty of Pharmacy, Department of Organic Chemistry, Budapest

Bemutatás módja

Szóbeli

Szekció

Pharmaceutical Sciences II. (Poster discussion will take place in the Aula during the Coffee Break)

Language of the presentation

Hungarian

Preferred session

Pharmaceutical Sciences

Összefoglaló szövege

Synthesis of modified β-peptide foldamers
Introduction: Foldamers are biomimetic polymers that can self-organize to form a regular secondary structure using secondary binding forces. The most important representatives of peptidomimetic foldamers are β-peptides. Unlike traditional α peptides, β peptide foldamers have the advantage of greater stability over proteolysis/metabolism and a more stable secondary structure. The α and β carbon atoms can be substitutable in a variety of ways, with which a high degree of structural diversity is caused, and this also has a decisive influence on conformation behavior.
Aims: In our work, we set ourselves the goal of producing foldamers in which these self-organizing structural units can be found between the dynamically variable ordered helix and between an unordered stretched conformation.
Method: To produce β peptide solid-phase peptide synthesis was used, in which we attached the first amino acid to a solid substrate (resin), then attached the next amino acid, and finally cleavage the finished sequence from the resin. After a retro-Diels-Alder reaction within the β peptide, we formed a double bond and obtained a compound with a stretched structure, not a helically arranged secondary structure. Performed a bromination in an aqueous solution, we received a bromine hidrine derivative, which allows for self-organization with a helical structure. If we treat the resulting molecule with metal zinc, we can get back the disordered structure containing a double bond. The cleaning of the molecule was carried out with a semi-preparatory HPLC of reverse phase (C18). This allowed us to separate pollutants and by-products from our sample.
Results: In the first step, we produced and cleaned the desired β peptide. In the second phase of our research, we successfully carried out the draft reactions, which were confirmed by analytical methods.
Conclusion: By periodically changing the above-mentioned reactions and conditions, we were able to create a dynamic structure, which can practically be considered a nano spring. For future applications, among others, it can play an important role in the creation of molecular machines and forces, which may even play a role in molecular surgery.


eeszter99@gmail.com
Semmelweis Egyetem, Semmelweis Egyetem Doktori Iskola, Gyógyszertudományok
Dr. Mándity István ,Ph.D.

University and Doctoral School

Semmelweis University, Doctoral School of Pharmaceutical Sciences

Supervisor

Dr. István Mándity, Ph.D.

Publication of my abstract

I give consent to the publication of my abstract on the website of the congress.

Kind

Szabad

Status

elfogadva

Accepted presentation method

szóbeli

Előadás fájl jóváhagyás

nem rendelkezett róla

Előadó

6940

Start

09:30

End

09:45

Authors (legacy)

Eszter Erdei
Research Centre for Natural Sciences, Institute of Materials and Environmental Chemistry, Artificial Transporters Research Group, Budapest
Semmelweis University, Faculty of Pharmacy, Department of Organic Chemistry, Budapest