Previous studies have described the concept of peptide strings in qualitative terms and illustrated it by applying its corrolaries in order to elucidate basic questions in oncology and rheumatology. The present investigation is the first to quantify these potential sub- and transcellular phenomena. Accordingly, the propagation of peptide strings is proposed here to occur by way of waves that in turn are subject to the energy equation established by Planck. As a result of these insights, widespread future applications can now be envisaged for peptide strings both in molecular medicine and quantum optics.
Deep Dive into Wave and quantum properties of peptide strings: defining a helix in spacetime.
Previous studies have described the concept of peptide strings in qualitative terms and illustrated it by applying its corrolaries in order to elucidate basic questions in oncology and rheumatology. The present investigation is the first to quantify these potential sub- and transcellular phenomena. Accordingly, the propagation of peptide strings is proposed here to occur by way of waves that in turn are subject to the energy equation established by Planck. As a result of these insights, widespread future applications can now be envisaged for peptide strings both in molecular medicine and quantum optics.
Over the past few years, the new interdisciplinary research fields of particle biology (1) and peptide strings (2-4) have been outlined. Moreover, the peptide strings concept was applied to develop novel views in the understanding and treatment of cancer (3,5), thereby expanding the epigenetic dimension of this disease (6), as well as of rheumatoid arthritis (7,8). It is conceivable that these qualitative descriptions primarily involving precisely defined elements of sub/transcellular protein dynamics, bioinformatics and peptide interactions might suffice for future translation into clinical practice. However, additional quantitative considerations could be crucial for successfully accomplishing such task and, furthermore, enlarge the scope of peptide strings beyond medicine. Therefore, an initial approximation towards this goal will be attempted here.
Among the key premises of the present quantitative definition of peptide strings is the fact that particles such as electrons have a dual nature in that they may also be perceived as waves (9).
Along similar lines, peptides represent, on the one hand, informational entities and particles in the sense of particle biology (1) or, as I would also coin them, biological quanta. In support of this view is the fact that single amino acids (e.g. glycine) are known to act, for instance, as neurotransmitters in synaptic clefts, but not across cells whereas protein molecules may translocate from one subcellular compartment to another and thereby influence cell fate by virtue of internal and/or external peptide signatures.
On the other hand, the peptides´ potential formation of peptide strings across cells follows a periodic character which ensures that a certain, e.g. oncogenic vs. antioncogenic (3)(4)(5)(6) or arthritogenic vs. anti-arthritogenic (7), peptide information is propagated sub-and transcellularly. Consequently, I propose that it is this periodicity that could represent the essence of a wave-like property of distinct peptide sequences resonating over large cellular distances and thus engendering a quantum state of coherence for a given period of time (Fig. 1).
Intrinsic to such state would be a certain energy value amenable to calculation through Planck´s equation (10), i.e. ε = h ν or, respectively, E = h f where E is the energy, h represents Planck´s constant and f designates the frequency, the latter of which is the ratio between the velocity v and the wavelength λ. The wavelength λ of such peptide string could in turn be calculated by applying de Broglie´s equation ( 9): λ = h/p whereby the impulse p is the product of the mass m and its velocity v. It follows therefrom that the peptide string wavelength λpep.str. may be determined as follows: λpep.str. = h/m v. More specifically, m would be here the mass of a given peptide capable of being propagated by means of a peptide string wave and v the latter´s sub/transcellular velocity. Based on a van der Waals distance of 3 Å between the contact residues of a distinct pair of interacting proteins and a duration of 1 ns for a protein´s conformational change (11) resulting from such interaction, I derive a (maximum) peptide string velocity of 0.3 m/s for a peptide with a mass of 1000 daltons which, according to above formula, would yield a (minimum) wavelength of approximately 10 Å, i.e. a value that is tenfold higher than that of the electron wavelength (9). Interestingly, this anticipated wavelength is close to the diameter range for proteins (11) which reflects the equally allosteric nature of peptide strings whereby the stimulus information is essentially transmitted through protein domains to yield a (peptide) replica of the stimulus that is then propagated in spacetime. Thereby, the energy transfer inherent to such process could conceivably be measured, e.g. in a manner analogous to previously described methods (12,13).
Given further that interactions between proteins involve changes in the electron structures of these molecules ( 14) which predictably result in modifications of their electromagnetic fields associated with the emission and/or absorption of photons, it is likely that light may be emitted and/or absorbed during the propagation of peptide strings.
Consequently, peptide strings might be used not only for therapeutic purposes (5)(6)(7)(8), but also in photonics where they could fundamentally extend the potential of peptides for transmitting photocurrent and acting as photodiodes (15).
Considering previous studies (3,4,7) and the present investigation together, I postulate the following 3 principles or laws of peptide strings:
Upon specific stimulation, a self-complementary peptide/protein (with potential for localization in 2 or more distinct subcellular compartments) relays the stimulus information through a stimulus-like region of its own that binds another selfcomplementary peptide/protein structurally both similar and complementary to the former one and so forth. This principle is
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