Comment; Antistaph activity at a micromolar & even nanomolar concentration is impressive!  The fact that it works against both methicillin sensitive & resistant strains is also noteworthy.  Looking at the ability of Multiple-Antibiotic Resistant Coagulase Negative Staph (MARCoNS) to cleave α-MSH leaving it ineffective brings us to a fascinating chemical battlefield important not only to the immune system, but to the entire NeuroEndocrine linked systems.


Alpha-melanocyte-stimulating hormone (α-MSH) is an endogenous neuropeptide that is known for its anti-inflammatory and antipyretic activities. We recently demonstrated that α-MSH possesses staphylocidal activity and causes bacterial membrane damage. To understand the role of its amino acid sequences in the staphylocidal mechanism, in the present study we investigated the antimicrobial activities of different fragments of α-MSH, i.e., α-MSH(6-13), α-MSH(11-13), and α-MSH(1-5), and compared them with that of the entire peptide. Our results showed that peptides containing the C-terminal region of α-MSH, namely, α-MSH(6-13) and α-MSH(11-13), efficiently killed >90% of both methicillin-sensitive and -resistant Staphylococcus aureus cells in the micromolar range and ∼50% of these cells in the nanomolar range; their efficiency was comparable to that of the entire α-MSH, whereas the peptide containing the N-terminal region, α-MSH(1-5), was found to be ineffective against S. aureus. The antimicrobial activity of α-MSH and its C-terminal fragments was not affected by the presence of NaCl or even divalent cations such as Ca2+ and Mg2+. Similar to the case for the parent peptide, α-MSH(6-13) and α-MSH(11-13) also depolarized and permeabilized Staphylococcus cells (∼70 to 80% of the cells were depolarized and lysed after 2 h of peptide exposure at micromolar concentrations). Furthermore, scanning and transmission electron microscopy showed remarkable morphological and ultrastructural changes on S. aureus cell surface due to exposure to α-MSH-based peptides. Thus, our observations indicate that C-terminal fragments of α-MSH retain the antimicrobial activity of entire peptide and that their mechanism of action is similar to that of full-length peptide. These observations are important and are critical in the rational design of α-MSH-based therapeutics with optimal efficacy.



The following are the works that has been done based on his request: 1.) Mailchimp opt in form 2.)Tesimonial form and recategorization 3.)Blog post categotized 4.)Duplicate SEO plugin deactivated i.e webtext tool 5.) Socia sharing duplicate removed 6.)Social sharing at the right buttom now sharing to his Facebook practice page And others All he need is to know how to use his website and i have sent him multiple screenshots of how to go about though he once complained to me he has poor eyesight. Please carefully go through our converstaion and his request and try and see that he is taking too much of my time unnecessarily because the site has all what he requested for now.

Dr. Raymond Oenbrink
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