1.

Ultrasound in phage display: a new approach to nonspecific elution

Authors: LUNDER, Mojca, BRATKOVIČ, Tomaž, URLEB, Uroš, KREFT, Samo, ŠTRUKELJ, Borut Description: A novel method for elution of peptide ligands from bacteriophage display libraries was developed by means of ultrasound in order to obtain selective peptides, eluted from target proteins.

COBISS.SI-ID: 2347377

2.

Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis

Authors: BRATKOVIČ, Tomaž, LUNDER, Mojca, URLEB, Uroš, ŠTRUKELJ, Borut. Description: By means of phage display, we succesfully isolated and characterized peptids that act as inhibitors of MurD and MurE enzymes in low micromolar concentration

COBISS.SI-ID: 2330225

3.

Progress in phage display: evolution of the technique and its applications

Author: BRATKOVIČ, Tomaž Description: The article deals with the broad review of the field of phage display with the emphasis on pharmaceutical and medical biotechnology. Some of our results are included as well.

COBISS.SI-ID: 2755697

4.

Engineered lactic acid bacterium Lactococcus lactis capable of binding antibodies and tumor necrosis factor alpha

Authors: RAVNIKAR, Matjaž, ŠTRUKELJ, Borut, OBERMAJER, Nataša, LUNDER, Mojca, BERLEC, Aleš Destcripition: Chronic inflammatory diseases are one of the most devastating modern malformanties.Tthe main cause for imflammation is TNFalpha.In order to block te acitvity of TNFalpha, we develope the recombinant Lactoccocus lactis by means of phage display that expresses the hipervariability peptidic domain at the surface.

COBISS.SI-ID: 24011815

5.

Cross-affinity of peptide ligands selected from phage display library against pancreatic phospholipase A2 and ammodytoxin C

Authors: GASER, Dominik, ŠTRUKELJ, Borut, BRATKOVIČ, Tomaž, KREFT, Samo, PUNGERČAR, Jože, LUNDER, Mojca Descripition: Two target proteins: ammodytoxin C and phospoholipase A2 were bound and several peptides were isolated from bacteriphage random peptide library against both proteins. The result indicates that both enzymes might have structurally similar epitopes.

COBISS.SI-ID: 2656113