Peptide phage display in biotechnology and biomedicine

Kuzmicheva, G. A.; Belyavskaya, V. A.

doi:10.1134/s1990750817010061

Cited by 10 publications

(3 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 3 The desired peptides for a given target having tailored chemical structures and activities can be obtained through appropriate genetics and chemical engineering. 4 Depending on their microstructure and functional groups, 5 diverse peptides have been developed for various applications in biomedicine, 6 bioengineering, and nanotechnology. 7 , 8 Because of their highly selective character and being relatively safe, peptides have been widely considered in pharmaceutical research.…”

Section: Introductionmentioning

confidence: 99%

α-Helical Antimicrobial Peptide Encapsulation and Release from Boron Nitride Nanotubes: A Computational Study

Dehaghani

Yousefi

Bagheri

et al. 2021

IJN

View full text Add to dashboard Cite

Introduction Antimicrobial peptides are potential therapeutics as anti-bacteria, anti-viruses, anti-fungi, or anticancers. However, they suffer from a short half-life and drug resistance which limit their long-term clinical usage. Methods Herein, we captured the encapsulation of antimicrobial peptide HA-FD-13 into boron nitride nanotube (BNNT) (20,20) and its release due to subsequent insertion of BNNT (14,14) with molecular dynamics simulation. Results The peptide-BNNT (20,20) van der Waals (vdW) interaction energy decreased to −270 kcal·mol −1 at the end of the simulation (15 ns). However, during the period of 0.2–1.8 ns, when half of the peptide was inside the nanotube, the encapsulation was paused due to an energy barrier in the vicinity of BNNT and subsequently the external intervention, such that the self-adjustment of the peptide allowed full insertion. The free energy of the encapsulation process was −200.12 kcal·mol −1 , suggesting that the insertion procedure occurred spontaneously. Discussion Once the BNNT (14,14) entered into the BNNT (20,20), the peptide was completely released after 83.8 ps. This revealed that the vdW interaction between the BNNT (14,14) and BNNT (20,20) was stronger than between BNNT (20,20) and the peptide; therefore, the BNNT (14,14) could act as a piston pushing the peptide outside the BNNT (20,20). Moreover, the sudden drop in the vdW energy between nanotubes to the value of the −1300 Kcal·mol −1 confirmed the self-insertion of the BNNT (14,14) into the BNNT (20,20) and correspondingly the release of the peptide.

show abstract

Section: Introductionmentioning

confidence: 99%

α-Helical Antimicrobial Peptide Encapsulation and Release from Boron Nitride Nanotubes: A Computational Study

Dehaghani

Yousefi

Bagheri

et al. 2021

IJN

View full text Add to dashboard Cite

show abstract

“…During the biopanning process, target‐selective phage modified with additional peptides are enriched from large phage peptide libraries (Pollmann et al, 2018). During the last decades, PSD has mainly been used in the medical field, especially for the discovery of diagnostic and therapeutic peptides (Kuzmicheva & Belyavskaya, 2017). Currently, the usability of PSD for solid‐ and inorganic material binding has proven to be successful not only in medicine applications but both in the nanotechnology and biomining fields (Braun et al, 2018; Care et al, 2015; Seker & Demir, 2011).…”

Section: Introductionmentioning

confidence: 99%

Identification of yttrium oxide‐specific peptides for future recycling of rare earth elements from electronic scrap

Maass,

Boelens,

Bloss

et al. 2024

Biotech & Bioengineering

View full text Add to dashboard Cite

Yttrium is a heavy rare earth element (REE) that acquires remarkable characteristics when it is in oxide form and doped with other REEs. Owing to these characteristics Y2O3 can be used in the manufacture of several products. However, a supply deficit of this mineral is expected in the coming years, contributing to its price fluctuation. Thus, developing an efficient, cost‐effective, and eco‐friendly process to recover Y2O3 from secondary sources has become necessary. In this study, we used phage surface display to screen peptides with high specificity for Y2O3 particles. After three rounds of enrichment, a phage expressing the peptide TRTGCHVPRCNTLS (DM39) from the random pVIII phage peptide library Cys4 was found to bind specifically to Y2O3, being 531.6‐fold more efficient than the wild‐type phage. The phage DM39 contains two arginines in the polar side chains, which may have contributed to the interaction between the mineral targets. Immunofluorescence assays identified that the peptide's affinity was strong for Y2O3 and negligible to LaPO4:Ce3+,Tb3+. The identification of a peptide with high specificity and affinity for Y2O3 provides a potentially new strategic approach to recycle this type of material from secondary sources, especially from electronic scrap.

show abstract

“…In recent years, the application of phage display has led to the discovery of many peptide structures, with targets ranging from inorganics and solids to carcinoma cells [6]. However, although successfully applied in the identification of many target-binding molecules, phage display is prone to errors and notoriously known for the identification of false positive hits [7].…”

Section: Introductionmentioning

confidence: 99%

Application of Next Generation Sequencing (NGS) in Phage Displayed Peptide Selection to Support the Identification of Arsenic-Binding Motifs

Braun

Schönberger

Vinke

et al. 2020

Viruses

View full text Add to dashboard Cite

Next generation sequencing (NGS) in combination with phage surface display (PSD) are powerful tools in the newly equipped molecular biology toolbox for the identification of specific target binding biomolecules. Application of PSD led to the discovery of manifold ligands in clinical and material research. However, limitations of traditional phage display hinder the identification process. Growth-based library biases and target-unrelated peptides often result in the dominance of parasitic sequences and the collapse of library diversity. This study describes the effective enrichment of specific peptide motifs potentially binding to arsenic as proof-of-concept using the combination of PSD and NGS. Arsenic is an environmental toxin, which is applied in various semiconductors as gallium arsenide and selective recovery of this element is crucial for recycling and remediation. The development of biomolecules as specific arsenic-binding sorbents is a new approach for its recovery. Usage of NGS for all biopanning fractions allowed for evaluation of motif enrichment, in-depth insight into the selection process and the discrimination of biopanning artefacts, e.g., the amplification-induced library-wide reduction in hydrophobic amino acid proportion. Application of bioinformatics tools led to the identification of an SxHS and a carboxy-terminal QxQ motif, which are potentially involved in the binding of arsenic. To the best of our knowledge, this is the first report of PSD combined with NGS of all relevant biopanning fractions.

show abstract

Peptide phage display in biotechnology and biomedicine

Cited by 10 publications

References 57 publications

α-Helical Antimicrobial Peptide Encapsulation and Release from Boron Nitride Nanotubes: A Computational Study

α-Helical Antimicrobial Peptide Encapsulation and Release from Boron Nitride Nanotubes: A Computational Study

Identification of yttrium oxide‐specific peptides for future recycling of rare earth elements from electronic scrap

Application of Next Generation Sequencing (NGS) in Phage Displayed Peptide Selection to Support the Identification of Arsenic-Binding Motifs

Contact Info

Product

Resources

About