Antimicrobial function of short amidated peptide fragments from the tick‐derived OsDef2 defensin

2019 ◽  
Vol 25 (12) ◽  
Author(s):  
Naadhira O. Ismail ◽  
Clerisa Odendaal ◽  
June C. Serem ◽  
Adam A. Strömstedt ◽  
Megan J. Bester ◽  
...  
Keyword(s):  
Peptide Fragments ◽  
Antimicrobial Function ◽  
Amidated Peptide

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

Effects of thrombin and its related peptide fragments on neutrophils

2018 ◽  
Author(s):  
Chun Hwee Lim
Keyword(s):  
Peptide Fragments ◽  
Related Peptide

Synthesis of hepatitis B surface antigen pre-S2 region fragments and studies on their immunogenicity

1988 ◽  
Vol 53 (11) ◽  
pp. 2952-2956 ◽  
Author(s):  
Bernard Lammek ◽  
Zbigniew Maćkiewicz ◽  
Izabela Derdowska ◽  
Hanna Świderska ◽  
Adam Nowosławski ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Solid Phase ◽  
Hepatitis B Surface Antigen ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Antigenic Determinants ◽  
Phase Method ◽  
Peptide Fragments ◽  
Humoral Immune

Two peptide fragments of hepatitis B surface antigen pre-S2 region were synthesized by the solid phase method. The peptides were purified by gel filtration or ion-exchange chromatography on Sephadex SP-C-25. Both peptides induced a cellular and humoral immune response in rabbits. The results showed that fragment 14-22 of pre-S2 region contains one of the antigenic determinants.

Semisynthesis of peptides - New strategy for specific protection and deprotection of the α-amino group of recombinantly-produced peptide fragments

1999 ◽  
Author(s):  
Johann M. Brass ◽  
Julie Frank ◽  
Fred W. Wagner ◽  
Hans Stocker ◽  
Erich Wünsch
Keyword(s):  
Amino Group ◽  
Peptide Fragments ◽  
New Strategy

scholarly journals Detection of Active BoNT/C and D by EndoPep-MS Using MALDI Biotyper Instrument and Comparison with the Mouse Test Bioassay

Toxins ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 10
Author(s):  
Ilenia Drigo ◽  
Elena Tonon ◽  
Simone Pascoletti ◽  
Fabrizio Anniballi ◽  
Suzanne R. Kalb ◽  
...  
Keyword(s):  
Limit Of Detection ◽  
Animal Health ◽  
Lethal Dose ◽  
Reference Method ◽  
Mouse Bioassay ◽  
Peptide Fragments ◽  
Mass Spectrometers ◽  
Detection And Identification ◽  
Maldi Biotyper ◽  
Sensitivity Specificity

Botulinum neurotoxins (BoNTs) are among the most poisonous known biological substances, and therefore the availability of reliable, easy-to use tools for BoNT detection are important goals for food safety and human and animal health. The reference method for toxin detection and identification is the mouse bioassay (MBA). An EndoPep-MS method for BoNT differentiation has been developed based on mass spectrometry. We have validated and implemented the EndoPep-MS method on a Bruker MALDI Biotyper for the detection of BoNT/C and D serotypes. The method was extensively validated using experimentally and naturally contaminated samples comparing the results with those obtained with the MBA. Overall, the limit of detection (LoD) for both C and D toxins were less than or equal to two mouse lethal dose 50 (mLD50) per 500 µL for all tested matrices with the exception of feces spiked with BoNT/C which showed signals not-related to specific peptide fragments. Diagnostic sensitivity, specificity and positive predictive value were 100% (95% CI: 87.66–100%), 96.08% (95% CI: 86.54–99.52%), and 93.33% (95% CI: 78.25–98.20%), respectively, and accuracy was 97.47% (95% CI: 91.15–99.69%). In conclusion, the tests carried out showed that the EndoPep-MS method, initially developed using more powerful mass spectrometers, can be applied to the Bruker MALDI Biotyper instrument with excellent results including for detection of the proteolytic activity of BoNT/C, BoNT/D, BoNT/CD, and BoNT/DC toxins.

scholarly journals Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Zhongqi He ◽  
Christopher P. Mattison ◽  
Dunhua Zhang ◽  
Casey C. Grimm
Keyword(s):  
Mass Spectrometry ◽  
Soluble Protein ◽  
Extraction Efficiency ◽  
Storage Proteins ◽  
Protein Composition ◽  
Protein Fractions ◽  
Peptide Fragments ◽  
2S Albumin ◽  
Cottonseed Protein ◽  
Glandless Cottonseed

AbstractIn this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tandem mass spectrometry identified peptide fragments from 336 proteins. While the majority of peptides were identified as belonging to vicilin and legumin storage proteins, peptides from other functional and uncharacterized proteins were also detected. Based on the types (unique peptide count) and relative abundance (normalized total ion current) of the polypeptides detected by mass spectrometry, we found lower levels (abundance) and types of legumin isoforms, but higher levels and more fragments of vicilin-like antimicrobial peptides in glandless samples, compared to glanded samples. Differences in peptide fragment patterns of 2S albumin and oleosin were also observed between glandless and glanded protein samples. These differences might be due to the higher extraction recovery of proteins from glandless cottonseed as proteins from glanded cottonseed tend to be associated with gossypol, reducing extraction efficiency. This work enriches the fundamental knowledge of glandless cottonseed protein composition. For practical considerations, this peptide information will be helpful to allow better understanding of the functional and physicochemical properties of glandless cottonseed protein, and improving the potential for food or feed applications.

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