Yi-Bo Shen | Searcharxiv

arXiv2025

$J/ψΛ$ femtoscopy and the nature of $P_{ψs}^Λ(4338)$

Over the past two decades, numerous exotic hadron states have been discovered, yet their underlying nature remains unclear. It is widely acknowledged that understanding hadron-hadron interactions is essential to unraveling their properties. Hadron spectroscopy is a powerful tool for this endeavor, providing rich experimental data that can shed light on exotic systems. Recently, the LHCb experiment analyzed the process $B^{-} \rightarrow J/ψΛ\bar{p}$ and observed a narrow peak in the $J/ψΛ$ invariant mass spectrum, regarding it as a candidate for a pentaquark. In this work, we extract the coupled-channel $J / ψΛ-\bar{D} Ξ_c-\bar{D}_s Λ_c$ potential based on the $J/ψΛ$ invariant mass spectrum. Our results indicate the existence of a bound state below the $\bar{D} Ξ_c$ mass threshold, corresponding to the experimentally measured state $P_{cs}(4338)$. Furthermore, we predict the scattering lengths and momentum correlation functions for the $J/ψΛ$ and $\bar{D}Ξ_c$ channels, which serve as theoretical references for future femtoscopy experiments.

hep-ph↗

arXiv2024

Implication of a negative effective range on the $D\bar{D}^*$ interaction and the nature of $X(3872)$

A recent analysis of the LHCb data [Phys. Rev. D 105 (2022) L031503] obtained a sizable negative effective range for the $X(3872)$. This has attracted intensive discussions on whether $X(3872)$ can be deemed as a $D\bar{D}^*$ molecular state. This work explicitly demonstrates that the negative effective range of the $X(3872)$ does not contradict the molecular picture, adopting an effective field theory formulation of the $D\bar{D}^*$ interaction that can simultaneously reproduce the binding energy and effective range of the $X(3872)$. We elaborate on the implications of the large negative effective range of $X(3872)$ and the small binding energy on the underlying $D\bar{D}^*$ interaction. Such results are relevant for a better understanding of hadronic molecules and their binding mechanism.

hep-ph↗